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bovine viral diarrhea virus polyprotein + H2O
?
DPNRKRGWPA + H2O
DPNRKR + GWPA
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-
-
-
?
DSSTKRGGSW + H2O
DSSTKR + GGSW
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preferred substrate, 33.5% cleavage, the active protease is able to cleave the substrate at the endoplasmic reticulum membrane in Huh-7 cells
-
-
?
FASGKRSQIG + H2O
FASGKR + SQIG
-
-
-
-
?
KPGLKRGGAK + H2O
KPGLKR + GGAK
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preferred substrate, 34.5% cleavage
-
-
?
LQYTKRGGVL + H2O
LQYTKR + GGVL
-
-
-
-
?
non-structural protein 4-5 + H2O
?
in trans-cleavage assays using NS4-5 as a substrate, NS3p acts as a fully functional protease that is able to process the polyprotein
-
-
?
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
Pyr-RTKR-7-amido-4-methylcoumarin + H2O
Pyr-RTKR + 7-amino-4-methylcoumarin
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-
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-
?
additional information
?
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bovine viral diarrhea virus polyprotein + H2O
?
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cleavages leading to the release of NS4A, NS4B, NS5A, and NS5B
-
?
bovine viral diarrhea virus polyprotein + H2O
?
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Leu at P1 is the only position conserved for all cleavage sites. At P1' alanine is found at the NS4A-NS4B site, whereas serine residues at this position at the NS3/NS4A, NS4B-NS5A, and NS5A/NS5B cleavage sites. For all cleavage sites the amino acids found at P1 and P1' are conserved for different genotypes of pestiviruses, despite the high degree of sequence variation found between these viruses
-
?
bovine viral diarrhea virus polyprotein + H2O
?
-
the enzyme is required for processing at nonstructural protein sites 3/4A, 4A/4B, 4B/5A and 5A/5B but not for cleavage at the junction between NS2 and NS3. A conserved Leu is found at the P1 position of all four cleavage sites, followed by either Ser (3/4A, 4B5A, and 5A/5B sites) or Ala (4A/4B site) at the P1' position
-
?
bovine viral diarrhea virus polyprotein + H2O
?
-
the enzyme is required for pestivirus replication. The enzyme is required for processing at nonstructural protein sites 3/4A, 4A/4B, 4B/5A and 5A/5B but not for cleavage at the junction between NS2 and NS3. A conserved Leu is found at the P1 position of all four cleavage sites, followed by either Ser (3/4A, 4B5A, and 5A/5B sites) or Ala (4A/4B site) at the P1' position
-
?
bovine viral diarrhea virus polyprotein + H2O
?
-
pestivirus P80 protein is a viral proteinase responsible for nonstructural polyprotein cleavage events
-
-
?
bovine viral diarrhea virus polyprotein + H2O
?
-
Leu at P1 is the only position conserved for all cleavage sites. At P1' alanine is found at the NS4A-NS4B site, whereas serine residues at this position at the NS3/NS4A, NS4B-NS5A, and NS5A/NS5B cleavage sites. For all cleavage sites the amino acids found at P1 and P1' are conserved for different genotypes of pestiviruses, despite the high degree of sequence variation found between these viruses
-
?
bovine viral diarrhea virus polyprotein + H2O
?
-
the enzyme is required for processing at nonstructural protein sites 3/4A, 4A/4B, 4B/5A and 5A/5B but not for cleavage at the junction between NS2 and NS3. A conserved Leu is found at the P1 position of all four cleavage sites, followed by either Ser (3/4A, 4B5A, and 5A/5B sites) or Ala (4A/4B site) at the P1' position
-
?
bovine viral diarrhea virus polyprotein + H2O
?
-
the enzyme is required for pestivirus replication. The enzyme is required for processing at nonstructural protein sites 3/4A, 4A/4B, 4B/5A and 5A/5B but not for cleavage at the junction between NS2 and NS3. A conserved Leu is found at the P1 position of all four cleavage sites, followed by either Ser (3/4A, 4B5A, and 5A/5B sites) or Ala (4A/4B site) at the P1' position
-
?
additional information
?
-
-
His1678, Asp1686 and Ser1752 constitute the catalytic triad
-
?
additional information
?
-
autocatalytic intramolecular cleavages of the enzyme, overview. Intramolecular cleavage of the peptide bond occurs between Leu1781 and Met1782 is required for activity, but cleavage of the Leu1748/Lys1749 peptide bond yields a proteolytically inactive NS3 fragment
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-
?
additional information
?
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pestiviral NS3 is a multifunctional molecule possessing protease, NTPase, and helicase activity
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-
?
additional information
?
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the enzyme is a natural protease-helicase fusion protein, structure-function analysis, overview
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-
?
additional information
?
-
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the enzyme is a natural protease-helicase fusion protein, structure-function analysis, overview
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-
?
additional information
?
-
the S1 pocket of the active site to accommodate the P1 residue (i.e., the immediate N-terminal residue of the cleavage site) is relatively deep and small, with a primarily hydrophobic environment, similar to the S1 pocket of HCV NS3. In contrast, the flavivirus NS3 P1 site is relatively flat and spacious but not as hydrophobic, substrate specificity, overview
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-
?
additional information
?
-
-
the S1 pocket of the active site to accommodate the P1 residue (i.e., the immediate N-terminal residue of the cleavage site) is relatively deep and small, with a primarily hydrophobic environment, similar to the S1 pocket of HCV NS3. In contrast, the flavivirus NS3 P1 site is relatively flat and spacious but not as hydrophobic, substrate specificity, overview
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-
?
additional information
?
-
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the NS3 protease of West nile virus has a cleavage sequence preference of (K/R)R-GG
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-
?
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(1S,5R)-6,6-dichloro-3-[cyclohexyl[[[(1,1-dimethylethyl)amino]carbonyl]amino]acetyl]-N-[1-[1,2-dioxo-2-(2-propenylamino)ethyl]butyl]-3-azabicyclo[3.1.0]hexan-2(S)-carboxamide
-
-
(2-[3-[(12-cyclohexyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo-[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carbonyl)amino]-2-oxohexanoylamino]acetylamino)phenylacetic acid
-
-
(2-[3-[(12-cyclohexyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo-[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carbonyl)amino]-2-oxohexanoylamino]acetylamino)phenylacetic acid tert-butyl ester
-
-
(2-[3-[(12-cyclohexyl-5,5-dimethyl-11,14-dioxo-2,6-dioxa-10,-13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carbonyl)amino]-2-oxohexanoylamino]acetylamino)phenylacetic acid tert-butyl ester
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1,1-dimethylethyl [1(S)-[[(1R,5S)-2(S)-[[[1-(cyclopropylmethyl)-3-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]-amino]-2-oxoethyl]amino]-2,3-dioxopropyl]amino]carbonyl]-6,6-dimethyl-3-azabicyclo[3.1.0]hexan-3-yl]carbonyl]-2,2-dimethylpropyl]carbamate
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SCH446211, potent ketoamide inhibitor. Has low oral bioavailability in rats and monkeys, but its subcutaneous pharmacokinetic profile is remarkable, with high AUC and 100% bioavailability in both species
1,1-dimethylethyl [1(S)-[[(1R,5S)-2(S)-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]-amino]-1,2-dioxoethyl]-4,4,4-trifluorobutyl]amino]carbonyl]-6,6-dimethyl-3-azabicyclo[3.1.0]hexan-3-yl]carbonyl]-2,2-dimethylpropyl]carbamate
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1,1-dimethylethyl [1(S)-[[(1R,5S)-2-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]amino]-1,2-dioxoethyl]pentyl]amino]carbonyl]-6,6-dimethyl-3-azabicyclo-[3.1.0]hexan-3-yl]carbonyl]-2,2-dimethylpropyl]carbamate
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1,1-dimethylethyl [1-cyclohexyl-2-[(1S,5R)-6,6-dichloro-2(S)-[[[1-[1,2-dioxo-2-(2-propenylamino) ethyl]butyl]-amino]carbonyl]-3-azabicyclo[3.1.0]hexan-3-yl]-2-oxoethyl]carbamate
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1,1-dimethylethyl [2-[(1S,5R)-2(S)-[[[1-(2-amino-1,2-dioxoethyl)butyl]amino]carbonyl]-6,6-dichloro-3-azabicyclo[3.1.0]hexan-3-yl]-1(S)-cyclohexyl-2-oxoethyl]-carbamate
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1,1-dimethylethyl[1-cyclohexyl-2-[(1S,5R)-6,6-dichloro-2(S)-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]amino]-1,2-dioxoethyl]-butyl]amino]carbonyl]-3-azabicyclo[3.1.0]hexan-3-yl]-2-oxoethyl]carbamate
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1,3,4-tri-O-galloyl-beta-D-glucose
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polyphenol compound from Saxifraga melanocentra
1,3,6-tri-O-galloyl-beta-D-glucose
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polyphenol compound from Terminalia chebula
1-O-(3-O-galloylgalloyl)-2,3,4-tri-O-galloyl-beta-D-glucose
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polyphenol compound from Saxifraga melanocentra
11-cyclohexyl-10,13-dioxo-2,5-dioxa-9,12-diazatricyclo[13.3.1.16,9]icosa-1(18),15(19),16-triene-8-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)-butyl)amide
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12-cyclohexyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(cyanophenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)-amide
-
-
12-cyclohexyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)amide
-
very potent inhibitor, S-isomer and R-isomer
12-cyclohexyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid (([1-(2-hydroxy-1-phenylethylcarbamoyl)methyl]aminooxalyl)butyl)-amide
-
-
12-cyclohexyl-11,14-dioxo-2-oxa-6-thia-10,13-diazatricyclo-[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)amide
-
-
12-cyclohexyl-5,5-dimethyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]-methyl)aminooxalyl)butyl)amide
-
-
12-cyclohexyl-5,5-dimethyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid (1-allylaminooxalylbutyl)amide
-
97% orally bioavailable
12-cyclohexyl-5,5-dimethyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid (1-aminooxalylbutyl)amide
-
-
12-cyclohexyl-6,6,11,14-tetraoxo-2-oxa-6lambda6-thia-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)-aminooxalyl)butyl)amide
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12-indan-2-yl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)amide
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12-isopropyl-5,5-dimethyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]-methyl)aminooxalyl)butyl)amide
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12-sec-butyl-5,5-dimethyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]-methyl)aminooxalyl)butyl)amide
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12-tert-butyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)amide
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12-tert-butyl-5,5-dimethyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)-aminooxalyl)butyl)amide
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-
2,2,2-trifluoro-1,1-dimethylethyl[2-[(1S,5R)-2(S)-[[[3-amino-1-(cyclobutylmethyl)-2,3-dioxopropyl]amino]-carbonyl]-6,6-dichloro-3-azabicyclo[3.1.0]hexan-3-yl]-1(S)-cyclohexyl-2-oxoethyl]carbamate
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2-methylpropyl [1(S)-cyclohexyl-2-[2(S)-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]-amino]-1,2-dioxoethyl]butyl]amino]carbonyl]-6,6-dimethyl-3-azabicyclo[3.1.0]hex-3-yl]-2-oxoethyl]carbamate
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-
2-methylpropyl [1(S)-[[(3aR,6aR)-4(S)-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]-amino]-1,2-dioxoethyl]butyl]amino]carbonyl]hexahydro-2,2-dimethyl-5H-furo[2,3-c]pyrrol-5-yl]carbonyl]-2,2-dimethylpropyl]carbamate
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2-methylpropyl [1(S)-[[(3aR,6aS)-1(S)-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]-amino]-1,2-dioxoethyl]butyl]amino]carbonyl]hexahydro-5,5-dimethylcyclopenta[c]pyrrol-2(1H)-yl]carbonyl]-2,2-dimethylpropyl]carbamate
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2-methylpropyl [1-cyclohexyl-2-[2-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1-phenylethyl]amino]-2-oxoethyl]amino]-1,2-dioxoethyl]butyl]amino]carbonyl]-4(S)-[(1,1-dimethylethyl)thio]-1-pyrrolidinyl]-2-oxoethyl]carbamate
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-
2-methylpropyl [1-cyclohexyl-2-[3(S)-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1-phenylethyl]amino]-2-oxoethyl]amino]-1,2-dioxoethyl]butyl]amino]carbonyl]-6,10-dithia-2-azaspiro[4.5]-decan-2-yl]-2-oxoethyl]carbamate
-
-
2-O-(4-O-galloylgalloyl)-1,3,4-tri-O-galloyl-beta-D-glucose
-
polyphenol compound from Rhodiola kirilowii
3,3'-digalloylprocyanidin B2
-
nonpeptide inhibitor of NS3-SP from Rhodiola kirilowii. Methylation and acylation of hydroxyl groups cause a decrease of activity
3,3'-digalloylproprodelphinidin B2
-
nonpeptide inhibitor of NS3-SP from Rhodiola kirilowii. Methylation and acylation of hydroxyl groups cause a decrease of activity
3,6-di-O-galloyl-beta-D-glucose
-
polyphenol compound from Saxifraga melanocentra
3-[2-(3-tert-butyl-ureido)-2-indan-2-yl-acetyl]-6,6-dichloro-3-aza-bicyclo[3.1.0]hexane-2-carboxylic acid(2-carbamoyl-1-cyclobutylmethyl-2-oxo-ethyl)-amide
-
-
3-[2-(3-tert-butyl-ureido)-3,3-dimethyl-butyryl]-6,6-dichloro-3-aza-bicyclo[3.1.0]hexane-2-carboxylic acid(2-carbamoyl-1-cyclobutylmethyl-2-oxo-ethyl)-amide
-
-
4-phenylphenacetyl-L-Lys-L-Lys-agmatine
-
competitive inhibitor
5,5-dimethyl-11,14-dioxo-12-phenyl-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]-methyl)aminooxalyl)butyl)amide
-
-
5-cyclohexyl-3,6-dioxo-11,16-dioxa-4,7-diazatricyclo[15.3.1.17,10]-docosa-1(21),17,19-triene-8-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)-amide
-
-
6,6-dichloro-3-[2-cyclohexyl-2-(3-cyclohexyl-ureido)-acetyl]-3-aza-bicyclo[3.1.0]hexane-2-carboxylic acid(2-carbamoyl-1-cyclobutylmethyl-2-oxo-ethyl)-amide
-
-
6-benzenesulfonyl-12-cyclohexyl-11,14-dioxo-2-oxa-6,10,13-triazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]-methyl)aminooxalyl)butyl)amide
-
-
epicatechin-3-O-gallate
-
nonpeptide inhibitor of NS3-SP from Rhodiola kirilowii. Methylation and acylation of hydroxyl groups cause a decrease of activity
epigallocatechin-3-O-gallate
-
nonpeptide inhibitor of NS3-SP from Rhodiola kirilowii. Methylation and acylation of hydroxyl groups cause a decrease of activity
N-acetyl-L-Lys-L-Lys-agmatine
-
-
N-[(2-methylpropoxy)carbonyl]-(S)-tert-leucyl-N-[1(S)-[2-[[2-[[2-(dimethylamino)-2-oxo-1-phenylethyl]amino]-2-oxoethyl]-amino]-1,2-dioxoethyl]butyl]-4(R)-methyl-(S)-prolinamide
-
-
N-[(2-methylpropoxy)carbonyl]-(S)-tert-leucyl-n-[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]amino]-1,2-dioxoethyl]butyl]-4(R)-(1,1-dimethylethoxy)-(S)-prolinamide
-
-
N-[(2-methylpropoxy)carbonyl]cyclohexylglucyl-N-[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]-amino]-1,2-dioxoethyl]butyl]prolinamide
-
-
N-[(2S)-6-amino-1-[(3S)-3-(carbamimidamidomethyl)pyrrolidin-1-yl]-1-oxohexan-2-yl]-N2-(biphenyl-4-ylacetyl)-L-lysinamide
-
-
N2-(biphenyl-4-ylacetyl)-L-lysyl-N-[(2E)-4-carbamimidamidobut-2-en-1-yl]-L-lysinamide
-
-
tert-butyl [(1S)-1-cyclohexyl-2-[(1S,5R)-6,6-dichloro-1-([4-cyclopropyl-1-[([[(1S)-3-(dimethylamino)-3-oxo-1-phenylpropyl]amino]methyl)amino]-3-oxobutyl]carbamoyl)-3-azabicyclo[3.1.0]hex-3-yl]-2-oxoethyl]carbamate
-
-
[1-[2-(2-carbamoyl-1-cyclobutylmethyl-2-oxo-ethylcarbamoyl)-6,6-dichloro-3-aza-bicyclo[3.1.0]hexane-3-carbonyl]-2,2-dimethyl-propyl]-carbamic acid tert-butyl ester
-
is the most promising of all inhibitors. Is more potent than SCH 503034. It has excellent potency in both enzyme and replicon assays. Demonstrates good overall pharmacokinetic profile with bioavailability above 10% in rat, monkey, and dog
[2-[2-(2-carbamoyl-1-cyclobutylmethyl-2-oxo-ethylcarbamoyl)-6,6-dichloro-3-aza-bicyclo[3.1.0]hex-3-yl]-1-indan-2-yl-2-oxo-ethyl]-carbamic acid tert-butyl ester
-
-
additional information
-
salidroside shows no activity up to 0.1 mM
-
additional information
-
two galloyl residues at 3 and 4 positions of glucopyranose ring of inhibitors are predicted to interact with Ser139, Gly137, Ala157, and Asp81 by hydrogen bond interaction and with Ala156 and Hie57 by hydrophobic interaction and to be essential for the activities of the series of inhibitors
-
additional information
-
specific allosteric contribution from the interaction interface between NS3 helicase and the protease domain
-
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African Horse Sickness
Expression of nonstructural protein NS3 of African horsesickness virus (AHSV): evidence for a cytotoxic effect of NS3 in insect cells, and characterization of the gene products in AHSV infected Vero cells.
African Horse Sickness
Membrane association of African horsesickness virus nonstructural protein NS3 determines its cytotoxicity.
African Horse Sickness
Subcellular localization of the nonstructural protein NS3 of African horsesickness virus.
African Horse Sickness
Variation of African horsesickness virus nonstructural protein NS3 in southern Africa.
Autoimmune Diseases
Hepatitis C virus nonstructural protein NS3 binds to Sm-D1, a small nuclear ribonucleoprotein associated with autoimmune disease.
Carcinogenesis
[Effect of hepatitis C virus nonstructural protein NS3 on telomerase activity]
Dengue
A single nine-amino acid peptide induces virus-specific, CD8+ human cytotoxic T lymphocyte clones of heterogeneous serotype specificities.
Dengue
Dengue virus-specific, human CD4+ CD8- cytotoxic T-cell clones: multiple patterns of virus cross-reactivity recognized by NS3-specific T-cell clones.
Dengue
Modulation of enzymatic activity of dengue virus nonstructural protein NS3 nucleoside triphosphatase/helicase by poly(U).
Encephalitis, Japanese
Japanese encephalitis virus nonstructural protein NS3 has RNA binding and ATPase activities.
Encephalitis, Tick-Borne
A short form of the tick-borne encephalitis virus NS3 protein.
Hepatitis C
Effect of hepatitis C virus nonstructural protein NS3 on proliferation and MAPK phosphorylation of normal hepatocyte line.
Hepatitis C
Heat-shock protein 90 is essential for stabilization of the hepatitis C virus nonstructural protein NS3.
Hepatitis C
Hepatitis C virus nonstructural protein NS3 binds to Sm-D1, a small nuclear ribonucleoprotein associated with autoimmune disease.
Hepatitis C
Hepatitis C virus nonstructural protein NS3 transforms NIH 3T3 cells.
Hepatitis C
IgE antibodies to hepatitis C virus core and nonstructural antigens in chronic hepatitis C patients before and after antiviral treatment.
Hepatitis C
Inhibition of sphingosine kinase by bovine viral diarrhea virus NS3 is crucial for efficient viral replication and cytopathogenesis.
Hepatitis C
Internal cleavage of hepatitis C virus NS3 protein is dependent on the activity of NS34A protease.
Hepatitis C
Product inhibition of the hepatitis C virus NS3 protease.
Hepatitis C
Screening factors effecting a response in soluble protein expression: formalized approach using design of experiments.
Hepatitis C
Significance of the immune response to a major, conformational B-cell epitope on the hepatitis C virus NS3 region defined by a human monoclonal antibody.
Hepatitis C
The DNA damage sensors ataxia-telangiectasia mutated kinase and checkpoint kinase 2 are required for hepatitis C virus RNA replication.
Hepatitis C
[Effect of hepatitis C virus nonstructural protein NS3 on telomerase activity]
Hepatitis C
[The combined application of nucleotide and amino acid sequences of NS3 hepatitis C virus protein, DNA encoding granulocyte macrophage colony-stimulating factor and inhibitor of regulatory T cells induces effective immune response against hepatitis C virus].
Hepatitis C, Chronic
IgE antibodies to hepatitis C virus core and nonstructural antigens in chronic hepatitis C patients before and after antiviral treatment.
Infections
Cytopathogenicity of border disease virus is correlated with integration of cellular sequences into the viral genome.
Infections
Dengue virus-specific, human CD4+ CD8- cytotoxic T-cell clones: multiple patterns of virus cross-reactivity recognized by NS3-specific T-cell clones.
Infections
Development of an immunochromatographic test kit for rapid detection of bovine viral diarrhea virus antigen.
Infections
Rescue of the highly virulent classical swine fever virus strain "Koslov" from cloned cDNA and first insights into genome variations relevant for virulence.
Infections
The DNA damage sensors ataxia-telangiectasia mutated kinase and checkpoint kinase 2 are required for hepatitis C virus RNA replication.
Infections
[Replication complex of tick-borne encephalitis complex. I. Identification of a nuclear fraction protein responsible for the initiation of RNA synthesis using affinity labeling]
Virus Diseases
An insect cell line derived from the small brown planthopper supports replication of Rice stripe virus, a tenuivirus.
Yellow Fever
Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein.
Yellow Fever
Interaction between the yellow fever virus nonstructural protein NS3 and the host protein Alix contributes to the release of infectious particles.
Yellow Fever
RNA-stimulated NTPase activity associated with yellow fever virus NS3 protein expressed in bacteria.
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0.0001
(1S,5R)-6,6-dichloro-3-[cyclohexyl[[[(1,1-dimethylethyl)amino]carbonyl]amino]acetyl]-N-[1-[1,2-dioxo-2-(2-propenylamino)ethyl]butyl]-3-azabicyclo[3.1.0]hexan-2(S)-carboxamide
-
-
0.00001
(2-[3-[(12-cyclohexyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo-[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carbonyl)amino]-2-oxohexanoylamino]acetylamino)phenylacetic acid
-
-
0.000044
(2-[3-[(12-cyclohexyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo-[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carbonyl)amino]-2-oxohexanoylamino]acetylamino)phenylacetic acid tert-butyl ester
-
-
0.000016
(2-[3-[(12-cyclohexyl-5,5-dimethyl-11,14-dioxo-2,6-dioxa-10,-13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carbonyl)amino]-2-oxohexanoylamino]acetylamino)phenylacetic acid tert-butyl ester
-
-
0.0000038
1,1-dimethylethyl [1(S)-[[(1R,5S)-2(S)-[[[1-(cyclopropylmethyl)-3-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]-amino]-2-oxoethyl]amino]-2,3-dioxopropyl]amino]carbonyl]-6,6-dimethyl-3-azabicyclo[3.1.0]hexan-3-yl]carbonyl]-2,2-dimethylpropyl]carbamate
-
SCH446211
0.000002
1,1-dimethylethyl [1(S)-[[(1R,5S)-2(S)-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]-amino]-1,2-dioxoethyl]-4,4,4-trifluorobutyl]amino]carbonyl]-6,6-dimethyl-3-azabicyclo[3.1.0]hexan-3-yl]carbonyl]-2,2-dimethylpropyl]carbamate
-
-
0.00001
1,1-dimethylethyl [1(S)-[[(1R,5S)-2-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]amino]-1,2-dioxoethyl]pentyl]amino]carbonyl]-6,6-dimethyl-3-azabicyclo-[3.1.0]hexan-3-yl]carbonyl]-2,2-dimethylpropyl]carbamate
-
-
0.0009
1,1-dimethylethyl [1-cyclohexyl-2-[(1S,5R)-6,6-dichloro-2(S)-[[[1-[1,2-dioxo-2-(2-propenylamino) ethyl]butyl]-amino]carbonyl]-3-azabicyclo[3.1.0]hexan-3-yl]-2-oxoethyl]carbamate
-
-
0.00002
1,1-dimethylethyl [2-[(1S,5R)-2(S)-[[[1-(2-amino-1,2-dioxoethyl)butyl]amino]carbonyl]-6,6-dichloro-3-azabicyclo[3.1.0]hexan-3-yl]-1(S)-cyclohexyl-2-oxoethyl]-carbamate
-
-
0.000015
1,1-dimethylethyl[1-cyclohexyl-2-[(1S,5R)-6,6-dichloro-2(S)-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]amino]-1,2-dioxoethyl]-butyl]amino]carbonyl]-3-azabicyclo[3.1.0]hexan-3-yl]-2-oxoethyl]carbamate
-
-
0.00003
11-cyclohexyl-10,13-dioxo-2,5-dioxa-9,12-diazatricyclo[13.3.1.16,9]icosa-1(18),15(19),16-triene-8-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)-butyl)amide
-
-
0.00031
12-cyclohexyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(cyanophenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)-amide
-
-
0.000008 - 0.0005
12-cyclohexyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)amide
0.00006
12-cyclohexyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid (([1-(2-hydroxy-1-phenylethylcarbamoyl)methyl]aminooxalyl)butyl)-amide
-
-
0.00001
12-cyclohexyl-11,14-dioxo-2-oxa-6-thia-10,13-diazatricyclo-[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)amide
-
-
0.000006
12-cyclohexyl-5,5-dimethyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]-methyl)aminooxalyl)butyl)amide
-
-
0.00053
12-cyclohexyl-5,5-dimethyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid (1-allylaminooxalylbutyl)amide
-
-
0.00022
12-cyclohexyl-5,5-dimethyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid (1-aminooxalylbutyl)amide
-
-
0.0033
12-cyclohexyl-6,6,11,14-tetraoxo-2-oxa-6lambda6-thia-10,13-diazatricyclo[14.3.1 .17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)-aminooxalyl)butyl)amide
-
-
0.00004
12-indan-2-yl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)amide
-
-
0.000019
12-isopropyl-5,5-dimethyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]-methyl)aminooxalyl)butyl)amide
-
-
0.00007
12-sec-butyl-5,5-dimethyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]-methyl)aminooxalyl)butyl)amide
-
-
0.000015 - 0.00013
12-tert-butyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)amide
0.000017
12-tert-butyl-5,5-dimethyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)-aminooxalyl)butyl)amide
-
-
0.000065
2,2,2-trifluoro-1,1-dimethylethyl[2-[(1S,5R)-2(S)-[[[3-amino-1-(cyclobutylmethyl)-2,3-dioxopropyl]amino]-carbonyl]-6,6-dichloro-3-azabicyclo[3.1.0]hexan-3-yl]-1(S)-cyclohexyl-2-oxoethyl]carbamate
-
-
0.00001
2-methylpropyl [1(S)-cyclohexyl-2-[2(S)-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]-amino]-1,2-dioxoethyl]butyl]amino]carbonyl]-6,6-dimethyl-3-azabicyclo[3.1.0]hex-3-yl]-2-oxoethyl]carbamate
-
-
0.00001
2-methylpropyl [1(S)-[[(3aR,6aR)-4(S)-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]-amino]-1,2-dioxoethyl]butyl]amino]carbonyl]hexahydro-2,2-dimethyl-5H-furo[2,3-c]pyrrol-5-yl]carbonyl]-2,2-dimethylpropyl]carbamate
-
-
0.000015
2-methylpropyl [1(S)-[[(3aR,6aS)-1(S)-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]-amino]-1,2-dioxoethyl]butyl]amino]carbonyl]hexahydro-5,5-dimethylcyclopenta[c]pyrrol-2(1H)-yl]carbonyl]-2,2-dimethylpropyl]carbamate
-
-
0.00012
2-methylpropyl [1-cyclohexyl-2-[2-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1-phenylethyl]amino]-2-oxoethyl]amino]-1,2-dioxoethyl]butyl]amino]carbonyl]-4(S)-[(1,1-dimethylethyl)thio]-1-pyrrolidinyl]-2-oxoethyl]carbamate
-
-
0.000028
2-methylpropyl [1-cyclohexyl-2-[3(S)-[[[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1-phenylethyl]amino]-2-oxoethyl]amino]-1,2-dioxoethyl]butyl]amino]carbonyl]-6,10-dithia-2-azaspiro[4.5]-decan-2-yl]-2-oxoethyl]carbamate
-
-
0.00003
3-[2-(3-tert-butyl-ureido)-2-indan-2-yl-acetyl]-6,6-dichloro-3-aza-bicyclo[3.1.0]hexane-2-carboxylic acid(2-carbamoyl-1-cyclobutylmethyl-2-oxo-ethyl)-amide
-
-
0.000007
3-[2-(3-tert-butyl-ureido)-3,3-dimethyl-butyryl]-6,6-dichloro-3-aza-bicyclo[3.1.0]hexane-2-carboxylic acid(2-carbamoyl-1-cyclobutylmethyl-2-oxo-ethyl)-amide
-
-
0.00205
4-phenylphenacetyl-L-Lys-L-Lys-agmatine
-
at pH 8.0 in Tris-HCl (10 mM), CHAPS (1 mM) and glycerol (20% v/v), at 25°C
0.000046
5,5-dimethyl-11,14-dioxo-12-phenyl-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]-methyl)aminooxalyl)butyl)amide
-
-
0.000007
5-cyclohexyl-3,6-dioxo-11,16-dioxa-4,7-diazatricyclo[15.3.1.17,10]-docosa-1(21),17,19-triene-8-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)-amide
-
-
0.000015
6,6-dichloro-3-[2-cyclohexyl-2-(3-cyclohexyl-ureido)-acetyl]-3-aza-bicyclo[3.1.0]hexane-2-carboxylic acid(2-carbamoyl-1-cyclobutylmethyl-2-oxo-ethyl)-amide
-
-
0.000036
6-benzenesulfonyl-12-cyclohexyl-11,14-dioxo-2-oxa-6,10,13-triazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]-methyl)aminooxalyl)butyl)amide
-
-
0.00014
N-[(2-methylpropoxy)carbonyl]-(S)-tert-leucyl-N-[1(S)-[2-[[2-[[2-(dimethylamino)-2-oxo-1-phenylethyl]amino]-2-oxoethyl]-amino]-1,2-dioxoethyl]butyl]-4(R)-methyl-(S)-prolinamide
-
-
0.000019
N-[(2-methylpropoxy)carbonyl]-(S)-tert-leucyl-n-[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]amino]-1,2-dioxoethyl]butyl]-4(R)-(1,1-dimethylethoxy)-(S)-prolinamide
-
-
0.01
N-[(2-methylpropoxy)carbonyl]cyclohexylglucyl-N-[1-[2-[[2-[[2-(dimethylamino)-2-oxo-1(S)-phenylethyl]amino]-2-oxoethyl]-amino]-1,2-dioxoethyl]butyl]prolinamide
-
-
0.0612
N-[(2S)-6-amino-1-[(3S)-3-(carbamimidamidomethyl)pyrrolidin-1-yl]-1-oxohexan-2-yl]-N2-(biphenyl-4-ylacetyl)-L-lysinamide
-
at pH 8.0 in Tris-HCl (10 mM), CHAPS (1 mM) and glycerol (20% v/v), at 25°C
0.02
N2-(biphenyl-4-ylacetyl)-L-lysyl-N-[(2E)-4-carbamimidamidobut-2-en-1-yl]-L-lysinamide
-
at pH 8.0 in Tris-HCl (10 mM), CHAPS (1 mM) and glycerol (20% v/v), at 25°C
0.000007
tert-butyl [(1S)-1-cyclohexyl-2-[(1S,5R)-6,6-dichloro-1-([4-cyclopropyl-1-[([[(1S)-3-(dimethylamino)-3-oxo-1-phenylpropyl]amino]methyl)amino]-3-oxobutyl]carbamoyl)-3-azabicyclo[3.1.0]hex-3-yl]-2-oxoethyl]carbamate
-
-
0.000009
[1-[2-(2-carbamoyl-1-cyclobutylmethyl-2-oxo-ethylcarbamoyl)-6,6-dichloro-3-aza-bicyclo[3.1.0]hexane-3-carbonyl]-2,2-dimethyl-propyl]-carbamic acid tert-butyl ester
-
-
0.00006
[2-[2-(2-carbamoyl-1-cyclobutylmethyl-2-oxo-ethylcarbamoyl)-6,6-dichloro-3-aza-bicyclo[3.1.0]hex-3-yl]-1-indan-2-yl-2-oxo-ethyl]-carbamic acid tert-butyl ester
-
-
0.000008
12-cyclohexyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)amide
-
S-isomer
0.0005
12-cyclohexyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)amide
-
R-isomer
0.000015
12-tert-butyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)amide
-
-
0.00013
12-tert-butyl-11,14-dioxo-2,6-dioxa-10,13-diazatricyclo[14.3.1.17,10]henicosa-1(19),16(20),17-triene-9-carboxylic acid ((([1-(dimethylcarbamoylphenylmethyl)carbamoyl]methyl)aminooxalyl)butyl)amide
-
-
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evolution
the enzyme is well conserved among the Flaviviridae
evolution
comparison of the Flaviviridae NS3 proteases
malfunction
-
antibody 3F10 disrupts the interaction between the cNS2B cofactor region and NS3 protease in vitro and reduces viral replication in HEK-293 cells
malfunction
deletion of Leu1781 results in enzyme inactivation
malfunction
altering either of the autocleavage sites (Leu192/Met193 and Leu159/Lys160) by Leu deletion or mutation greatly inhibits RNA replication in a CSFV replicon system and results in a loss of genome RNA infectivity
malfunction
the gain of function mutation 3/V132A as well as the mutations in the NS4A-kink region expose the TEV cleavage site suggesting a destabilization of the NS3/4A-kink interaction. Single mutations at the NS3/4A-kink interface allow for polyprotein processing and RNA replication. The gain of function mutation 3/V132A can be functionally substituted by the single mutations 4A/L45A or 4A/Y47A in NS2-3-independent virion morphogenesis. The replication-deficient NS3/4A double mutant 4A/L45-Y47-AA is functional in viral packaging when supplied in trans. Analysis of NS3 and NS2 mutations combined, overview
metabolism
internal cleavage within the NS3 moiety is a common process that further extends the functional repertoires of the multifunctional NS2-3 or NS3 and represents another level of the complex polyprotein processing of Flaviviridae
metabolism
upon infection of the host cell the viral RNA genome is translated into a polyprotein that is processed by cellular and viral proteases into the mature structural (SP) and nonstructural (NS) proteins. For members of the genus Pestivirus the array in the polyprotein is the following: NH2-Npro (N-terminal autoprotease), C (capsid protein, core), Erns (envelope protein RNase secreted), E1, E2, p7, NS2-3 (NS2 and NS3), NS4A, NS4B, NS5A, NS5B-COOH. The N-terminal autoprotease Npro generates its own C-terminus and thereby the N-terminus of the capsid protein core (C). Further cleavages releasing the structural proteins C, Erns, E1 and E2 as well as p7 are mediated by proteases residing in the endoplasmatic reticulum (ER). The cleavage between NS2 and NS3 is catalyzed by an autoprotease in NS2. The activity of the NS2 protease is temporally regulated by a cellular cofactor leading to significant amounts of uncleaved NS2-3 in pestivirus infected cells. The cleavages downstream of NS3, NS4A, NS4B and NS5A are catalyzed by the serine protease domain of NS3 which requires NS4A as cofactor for full proteolytic activity and is termed NS3-4A protease
physiological function
nonstructural protein 3, NS3, is a nonstructural protein possessing serine protease, helicase, and NTPase activity, it is a key player in virus replication. Ability of NS3 of classical swine fever virus to compensate for disabling size increase of core protein, role of NS3 in particle assembly, overview. In addition to its essential role in RNA replication, NS3 apparently organizes the incorporation of RNA into budding virus particles
physiological function
pivotal for processing of a large portion of the viral polyprotein is a serine protease activity within nonstructural protein 3 that also harbors helicase and NTPase activities essential forRNA replication
physiological function
cleavages downstream of NS3, NS4A, NS4B and NS5A, former parts of the viral polyprotein, are catalyzed by the serine protease domain of NS3 which requires NS4A as cofactor for full proteolytic activity and is termed NS3-4A protease. A special feature of pestiviruses is the existence of significant amounts of uncleaved NS2-3 in the infected cell and its essential role in virion formation, temporal restriction of NS2-3 processing by the NS2 autoprotease, mostly restricted to the early phase of infection. NS2-3 translated at later time points is only inefficiently processed leading to the accumulation of uncleaved NS2-3 which temporally correlates with the onset of virion morphogenesis. Downregulation of NS2-3 processing plays a crucial role for the non-cytopathogenic (ncp) biotype of pestiviruses in cell culture
physiological function
NS3 is a multifunctional enzyme and a natural fusion of an N-terminal chymotrypsin-like serine protease and a C-terminal nucleotide triphosphatase (NTPase)/helicase. All Flaviviridae NS3 proteases require a segment of another viral protein, NS4A for pestiviruses, as the structurally integrated essential cofactor, termed protease cofactor segment (PCS) to fulfill the protease function, and for pestiviruses the protease is responsible for the cleavage of all the linkages in the NS3-NS4A-NS4B-NS5A-NS5B region of the viral polyprotein. The enzyme is a natural protease-helicase fusion protein, structure-function analysis, overview. Analysis of the mechanism of NS3 helicase regulation by its fusion partner protease
additional information
structure-function analysis suggests that NS3/4A can adopt two different conformations in the infected cell, a closed form that is used in RNA replication complexes and a more open conformation functional in viral assembly. Furthermore, the NS2-3/4A complex, required for virion assembly of prototype pestiviruses, displays a similar open conformation. CSFV NS3/4A complex crystal structure analysis, overview
additional information
the catalytic triad is formed by residues H69, D97, and S163. The intramolecular interface between protease and helicase in CSFV NS3 is featured by three clusters of interactions, overview
additional information
-
the catalytic triad is formed by residues H69, D97, and S163. The intramolecular interface between protease and helicase in CSFV NS3 is featured by three clusters of interactions, overview
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Xu, J.; Mendez, E.; Caron, P.R.; Lin, C.; Murcko, M.A.; Collett, M.S.; Rice, C.M.
Bovine viral diarrhea virus NS3 serine proteinase: polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replication
J. Virol.
71
5312-5322
1997
Bovine viral diarrhea virus 1, Bovine viral diarrhea virus 1 NADL
brenda
Tautz, N.; Elbers, K.; Stoll, D.; Meyers, G.; Thiel, H.J.
Serine protease of pestiviruses: determination of cleavage sites
J. Virol.
71
5415-5422
1997
Bovine viral diarrhea virus 1, Bovine viral diarrhea virus 1 CP7
brenda
Deng, R.; Brock, K.V.
Molecular cloning and nucleotide sequence of a pestivirus genome, noncytopathic bovine viral diarrhea virus strain SD-1
Virology
191
867-869
1992
Bovine viral diarrhea virus 1 (Q01499), Bovine viral diarrhea virus 1 SD-1 (Q01499)
brenda
Tautz, N.; Kaiser, A.; Thiel, H.J.
NS3 serine protease of bovine viral diarrhea virus: characterization of active site residues, NS4A cofactor domain, and protease-cofactor interactions
Virology
273
351-363
2000
Bovine viral diarrhea virus 1
brenda
Chen, K.X.; Njoroge, F.G.; Arasappan, A.; Venkatraman, S.; Vibulbhan, B.; Yang, W.; Parekh, T.N.; Pichardo, J.; Prongay, A.; Cheng, K.C.; Butkiewicz, N.; Yao, N.; Madison, V.; Girijavallabhan, V.
Novel potent hepatitis C virus NS3 serine protease inhibitors derived from proline-based macrocycles
J. Med. Chem.
49
995-1005
2006
Hepacivirus C
brenda
Wiskerchen, M.; Collett, M.S.
Pestvirus gene expression: protein p80 of bovine viral diarrhea virus is a proteinase involved in polyprotein processing
Virology
184
341-350
1991
Bovine viral diarrhea virus 1
brenda
Zuo, G.; Li, Z.; Chen, L.; Xu, X.
Activity of compounds from Chinese herbal medicine Rhodiola kirilowii (Regel) Maxim against HCV NS3 serine protease
Antiviral Res.
76
86-92
2007
Hepacivirus C
brenda
Li, X.; Zhang, W.; Qiao, X.; Xu, X.
Prediction of binding for a kind of non-peptic HCV NS3 serine protease inhibitors from plants by molecular docking and MM-PBSA method
Bioorg. Med. Chem.
15
220-226
2007
Hepacivirus C
brenda
Chen, K.X.; Vibulbhan, B.; Yang, W.; Cheng, K.C.; Liu, R.; Pichardo, J.; Butkiewicz, N.; Njoroge, F.G.
Potent and selective small molecule NS3 serine protease inhibitors of Hepatitis C virus with dichlorocyclopropylproline as P2 residue
Bioorg. Med. Chem.
16
1874-1883
2008
Hepacivirus C
brenda
Beran, R.K.; Serebrov, V.; Pyle, A.M.
The serine protease domain of hepatitis C viral NS3 activates RNA helicase activity by promoting the binding of RNA substrate
J. Biol. Chem.
282
34913-34920
2007
Hepacivirus C
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