1bt7
From Proteopedia
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Revision as of 13:51, 5 November 2007
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THE SOLUTION NMR STRUCTURE OF THE N-TERMINAL PROTEASE DOMAIN OF THE HEPATITIS C VIRUS (HCV) NS3-PROTEIN, FROM BK STRAIN, 20 STRUCTURES
Overview
The solution structure of the hepatitis C virus (BK strain) NS3 protein, N-terminal domain (186 residues) has been solved by NMR spectroscopy. The, protein is a serine protease with a chymotrypsin-type fold, and is, involved in the maturation of the viral polyprotein. Despite the knowledge, that its activity is enhanced by the action of a viral protein cofactor, NS4A, the mechanism of activation is not yet clear. The analysis of the, folding in solution and the differences from the crystallographic, structures allow the formulation of a model in which, in addition to the, NS4A cofactor, the substrate plays an important role in the activation of, the catalytic mechanism. A unique structural feature is the presence of a, zinc-binding site exposed on the surface, subject to a slow conformational, exchange process.
About this Structure
1BT7 is a Single protein structure of sequence from Gb virus c with ZN as ligand. Structure known Active Sites: CTS and ZNB. Full crystallographic information is available from OCA.
Reference
The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism., Barbato G, Cicero DO, Nardi MC, Steinkuhler C, Cortese R, De Francesco R, Bazzo R, J Mol Biol. 1999 Jun 4;289(2):371-84. PMID:10366511
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