Literature summary for 3.4.21.91 extracted from

Luo, D.; Vasudevan, S.G.; Lescar, J.
The flavivirus NS2B-NS3 protease-helicase as a target for antiviral drug development (2015), Antiviral Res., 118, 148-158 .

Search for more literature for 3.4.21.91

Application

Application	Comment	Organism
drug development	flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development	Japanese encephalitis virus
drug development	flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development	Dengue virus type 4
drug development	flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development	Yellow fever virus
drug development	flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development	West Nile virus
drug development	flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development	Murray Valley encephalitis virus
drug development	flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development	Kunjin virus
drug development	flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development	Dengue virus type 2
drug development	flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development	dengue virus type I
drug development	flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development	Dengue virus type 3
drug development	flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development	Kokobera virus

Crystallization (Commentary)

Crystallization (Comment)	Organism
analysis of enzyme structure, PDB ID 2QEQ	Kunjin virus
analysis of enzyme structure, PDB ID 2Z83	Japanese encephalitis virus
analysis of enzyme structures, PDB IDs 1YKS and 1YMF	Yellow fever virus
analysis of enzyme structures, PDB IDs 2FOM, 2M9P, 2M9Q, 2BHR, and 2BMF	Dengue virus type 2
analysis of enzyme structures, PDB IDs 2JLQ, 2JLR, 2JLU, 2JLV, 2JLW, 2JLX, 2JLY, 2JLZ, 2WHX, 2WZQ, and 2VBC	Dengue virus type 4
analysis of enzyme structures, PDB IDs 2V6I and 2V6J	Kokobera virus
analysis of enzyme structures, PDB IDs 2V8O and 2WV9	Murray Valley encephalitis virus
analysis of enzyme structures, PDB IDs 2YOL, 3E90, 2FP7, 2IJO, and 2GGV	West Nile virus
analysis of enzyme structures, PDB IDs 3L6P and 3LKW	dengue virus type I
analysis of enzyme structures, PDB IDs 3U1I and 3U1J	Dengue virus type 3

Inhibitors

Inhibitors	Comment	Organism
Aprotinin	bovine pancreatic trypsin inhibitor, BPTI	Dengue virus type 3
Aprotinin	bovine pancreatic trypsin inhibitor, BPTI	West Nile virus
additional information	enzyme ligand binding structure analysis	Dengue virus type 2
additional information	enzyme ligand binding structure analysis	Dengue virus type 3
additional information	enzyme ligand binding structure analysis	Dengue virus type 4
additional information	enzyme ligand binding structure analysis	dengue virus type I
additional information	enzyme ligand binding structure analysis	Japanese encephalitis virus
additional information	enzyme ligand binding structure analysis	Kokobera virus
additional information	enzyme ligand binding structure analysis	Kunjin virus
additional information	enzyme ligand binding structure analysis	Murray Valley encephalitis virus
additional information	enzyme ligand binding structure analysis	West Nile virus
additional information	enzyme ligand binding structure analysis	Yellow fever virus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
additional information	the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein	Japanese encephalitis virus	-	-
additional information	the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein	Dengue virus type 4	-	-
additional information	the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein	Yellow fever virus	-	-
additional information	the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein	West Nile virus	-	-
additional information	the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein	Murray Valley encephalitis virus	-	-
additional information	the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein	Kunjin virus	-	-
additional information	the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein	Dengue virus type 2	-	-
additional information	the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein	dengue virus type I	-	-
additional information	the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein	Dengue virus type 3	-	-
additional information	the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein	Kokobera virus	-	-

Organism

Organism	UniProt	Comment	Textmining
Dengue virus type 2	P29990	DENV2	-
Dengue virus type 2 Thailand/16681/1984	P29990	DENV2	-
Dengue virus type 3	Q6YMS3	genome polyprotein; DENV3	-
Dengue virus type 3 Martinique/1243/1999	Q6YMS3	genome polyprotein; DENV3	-
Dengue virus type 4	Q2YHF0	genome polyprotein; DENV4	-
Dengue virus type 4 Thailand/0348/1991	Q2YHF0	genome polyprotein; DENV4	-
dengue virus type I	P17763	genome polyprotein; DENV1	-
dengue virus type I Nauru/West Pac/1974	P17763	genome polyprotein; DENV1	-
Japanese encephalitis virus	P27395	genome polyprotein; JEV	-
Japanese encephalitis virus SA-14	P27395	genome polyprotein; JEV	-
Kokobera virus	Q32ZD5	genome polyprotein; KOKV	-
Kunjin virus	P14335	genome polyprotein	-
Kunjin virus MRM61C	P14335	genome polyprotein	-
Murray Valley encephalitis virus	P05769	genome polyprotein; MVEV	-
Murray Valley encephalitis virus MVE-1-51	P05769	genome polyprotein; MVEV	-
West Nile virus	P06935	genome polyprotein; WNV	-
Yellow fever virus	P03314	YFV	-
Yellow fever virus 17D vaccine	P03314	YFV	-

Synonyms

Synonyms	Comment	Organism
NS2B-NS3 protease-helicase	-	Japanese encephalitis virus
NS2B-NS3 protease-helicase	-	Dengue virus type 4
NS2B-NS3 protease-helicase	-	Yellow fever virus
NS2B-NS3 protease-helicase	-	West Nile virus
NS2B-NS3 protease-helicase	-	Murray Valley encephalitis virus
NS2B-NS3 protease-helicase	-	Kunjin virus
NS2B-NS3 protease-helicase	-	Dengue virus type 2
NS2B-NS3 protease-helicase	-	dengue virus type I
NS2B-NS3 protease-helicase	-	Dengue virus type 3
NS2B-NS3 protease-helicase	-	Kokobera virus

Cofactor

Cofactor	Comment	Organism
NS2B cofactor	N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease	Japanese encephalitis virus
NS2B cofactor	N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease	Dengue virus type 4
NS2B cofactor	N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease	Yellow fever virus
NS2B cofactor	N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease	West Nile virus
NS2B cofactor	N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease	Murray Valley encephalitis virus
NS2B cofactor	N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease	Kunjin virus
NS2B cofactor	N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease	Dengue virus type 2
NS2B cofactor	N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease	dengue virus type I
NS2B cofactor	N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease	Dengue virus type 3
NS2B cofactor	N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease	Kokobera virus

General Information

General Information	Comment	Organism
additional information	enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis	Japanese encephalitis virus
additional information	enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis	Dengue virus type 4
additional information	enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis	Yellow fever virus
additional information	enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis	West Nile virus
additional information	enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis	Murray Valley encephalitis virus
additional information	enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis	Kunjin virus
additional information	enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis	Dengue virus type 2
additional information	enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis	dengue virus type I
additional information	enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis	Dengue virus type 3
additional information	enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis	Kokobera virus
physiological function	the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response	Japanese encephalitis virus
physiological function	the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response	Dengue virus type 4
physiological function	the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response	Yellow fever virus
physiological function	the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response	West Nile virus
physiological function	the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response	Murray Valley encephalitis virus
physiological function	the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response	Kunjin virus
physiological function	the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response	Dengue virus type 2
physiological function	the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response	dengue virus type I
physiological function	the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response	Dengue virus type 3
physiological function	the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response	Kokobera virus