1BT7

THE SOLUTION NMR STRUCTURE OF THE N-TERMINAL PROTEASE DOMAIN OF THE HEPATITIS C VIRUS (HCV) NS3-PROTEIN, FROM BK STRAIN, 20 STRUCTURES

1BT7 の概要

• エントリーDOI: 10.2210/pdb1bt7/pdb
• 分子名称: NS3 SERINE PROTEASE, ZINC ION (2 entities in total)
• 機能のキーワード: hydrolase, viral non-structural protein, serine protease
• 由来する生物種: Hepatitis C virus
• 細胞内の位置: Core protein p21: Host endoplasmic reticulum membrane; Single-pass membrane protein. Core protein p19: Virion (By similarity). Envelope glycoprotein E1: Virion membrane; Single-pass type I membrane protein (Potential). Envelope glycoprotein E2: Virion membrane; Single-pass type I membrane protein (Potential). p7: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Protease NS2-3: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein (By similarity). Non-structural protein 4A: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential). Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Non-structural protein 5A: Host endoplasmic reticulum membrane; Peripheral membrane protein (By similarity). RNA-directed RNA polymerase: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential): P26663
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19699.94

構造登録者

Barbato, G.,Cicero, D.O.,Nardi, M.C.,Steinkuhler, C.,Cortese, R.,De Francesco, R.,Bazzo, R. (登録日: 1998-09-01, 公開日: 1999-06-22, 最終更新日: 2024-05-22)

主引用文献

Barbato, G.,Cicero, D.O.,Nardi, M.C.,Steinkuhler, C.,Cortese, R.,De Francesco, R.,Bazzo, R.
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.
J.Mol.Biol., 289:371-384, 1999

PubMed Abstract: 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.

PubMed: 10366511
DOI: 10.1006/jmbi.1999.2745

実験手法

SOLUTION NMR