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1a1q
From Proteopedia
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HEPATITIS C VIRUS NS3 PROTEINASE
Overview
During replication of hepatitis C virus (HCV), the final steps of, polyprotein processing are performed by a viral proteinase located in the, N-terminal one-third of nonstructural protein 3. The structure of NS3, proteinase from HCV BK strain was determined by X-ray crystallography at, 2.4 angstrom resolution. NS3P folds as a trypsin-like proteinase with two, beta barrels and a catalytic triad of His-57, Asp-81, Ser-139. The, structure has a substrate-binding site consistent with the cleavage, specificity of the enzyme. Novel features include a structural, zinc-binding site and a long N-terminus that interacts with neighboring, molecules by binding to a hydrophobic surface patch.
About this Structure
1A1Q is a Single protein structure of sequence from Hepatitis c virus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site., Love RA, Parge HE, Wickersham JA, Hostomsky Z, Habuka N, Moomaw EW, Adachi T, Hostomska Z, Cell. 1996 Oct 18;87(2):331-42. PMID:8861916
Page seeded by OCA on Tue Nov 20 10:33:23 2007
