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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

机译:丙型肝炎病毒(HCV)NS3蛋白N末端蛋白酶结构域的溶液结构为其激活和催化机制提供了新见解

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摘要

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.
机译:丙型肝炎病毒(BK株)NS3蛋白N末端域(186个残基)的溶液结构已通过NMR光谱解析。该蛋白是具有胰凝乳蛋白酶类型折叠的丝氨酸蛋白酶,并参与病毒多蛋白的成熟。尽管已知其活性通过病毒蛋白辅因子NS4A的作用而增强,但激活机制尚不清楚。通过分析溶液中的折叠以及与晶体结构的差异,可以建立模型,其中除NS4A辅因子外,底物在催化机理的激活中也起着重要作用。独特的结构特征是表面上存在一个锌结合位点,经历缓慢的构象交换过程。

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