PMID:8861917

Citation	Kim, JL, Morgenstern, KA, Lin, C, Fox, T, Dwyer, MD, Landro, JA, Chambers, SP, Markland, W, Lepre, CA, O'Malley, ET, Harbeson, SL, Rice, CM, Murcko, MA, Caron, PR and Thomson, JA (1996) Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide. Cell 87:343-55
Abstract	An estimated 1% of the global human population is infected by hepatitis C viruses (HCVs), and there are no broadly effective treatments for the debilitating progression of chronic hepatitis C. A serine protease located within the HCV NS3 protein processes the viral polyprotein at four specific sites and is considered essential for replication. Thus, it emerges as an attractive target for drug design. We report here the 2.5 angstrom resolution X-ray crystal structure of the NS3 protease domain complexed with a synthetic NS4A activator peptide. The protease has a chymotrypsin-like fold and features a tetrahedrally coordinated metal ion distal to the active site. The NS4A peptide intercalates within a beta sheet of the enzyme core.
Links	PubMed
Keywords	Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; Enzyme Activation; Hepacivirus/enzymology; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Conformation; Sequence Alignment; Substrate Specificity; Viral Nonstructural Proteins/metabolism; Viral Nonstructural Proteins/ultrastructure; Zinc
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
HCVH:POLG	enables	GO:0004252: serine-type endopeptidase activity	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
HCVH:POLG	enables	GO:0008270: zinc ion binding	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete

References

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