This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1bt7
From Proteopedia
|
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
Page seeded by OCA on Mon Nov 5 15:27:18 2007
