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Literature summary for 3.4.21.98 extracted from

  • Kim, J.L.; Morgenstern, K.A.; Lin, C.; Fox, T.; Dwyer, M.D.; Landro, J.A.; Chambers, S.P.; Markland, W.; Lepre, C.A.; OµMalley, E.T.; Harbeson, S.L.; Rice, C.M.; Murcko, M.A.; Caron, P.R.; Thomson, J.A.
    Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide [published erratum appears in Cell 1997 Apr 4;89(1):159 (1996), Cell, 87, 343-355.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
NS4A NS4A is a 54 residue amphipathic peptide acting as a cofactor and possibly assisting the membrane-localization of NS3 Hepacivirus C
NS4A enhances the activity of NS3 protease in all cleavages via the formation of an NS3/NS4A Hepacivirus C

Cloned(Commentary)

Cloned (Comment) Organism
residues 1027-1207 of the NS3 protein, expressed in Escherichia coli Hepacivirus C

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of a recombinant truncated HCV NS3 protease domain complexed with a synthetic peptide encompassing the essential NS3-binding region of NS4A at 2.5 A resolution Hepacivirus C

Metals/Ions

Metals/Ions Comment Organism Structure
Zinc His149 may be an integral part of zinc coordination, may have a structural rather than a catalytic role, effects on protein folding or post-folding stability Hepacivirus C

Organism

Organism UniProt Comment Textmining
Hepacivirus C
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Hepacivirus C