Domain 3 of non-structural protein 5A from hepatitis C virus is natively unfolded

被引：72

作者：

Hanoulle, Xavier ^{[1
]}

Verdegem, Dries ^{[1
]}

Badillo, Aurelie ^{[2
]}

Wieruszeski, Jean-Michel ^{[1
]}

Penin, Francois ^{[2
]}

Lippens, Guy ^{[1
]}

机构：

[1] Univ Sci & Technol Lille, UGSF, CNRS, UMR 8576,IFR 147, F-59655 Villeneuve Dascq, France

[2] Univ Lyon, IBCP, CNRS, UMR 5086,IFR 128 BioSci Gerland Lyon Sud, F-69397 Lyon, France

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2009年 / 381卷 / 04期

关键词：

Hepatitis C virus; NS5A; Domain; 3; NMR; Unstructured; Circular dichroism; NMR ASSIGNMENT; NS5A; BINDING; IDENTIFICATION; REPLICATION; BIOLOGY;

D O I：

10.1016/j.bbrc.2009.02.108

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Hepatitis C virus (HCV) non-structural protein 5A (NS5A) is involved both in the viral replication and particle production. Its third domain (NS5A-D3), although not absolutely required for replication, is a key determinant for the production and assembly of novel HCV particles. As a prerequisite to elucidate the precise functions of this domain, we report here the first molecular characterization of purified recombinant HCV NS5A-D3. Sequence analysis indicates that NS5A-D3 is mostly unstructured but that short structural elements may exist at its N-terminus. Gel filtration chromatography, circular dichroism and finally NMR spectroscopy all point out the natively unfolded nature of purified recombinant NS5A-D3. This lack of stable folding is thought to be essential for primary interactions of NS5A-D3 domain with other viral or host proteins, which could stabilize some specific conformations conferring new functional features. (C) 2009 Elsevier Inc. All rights reserved.

引用

页码：634 / 638

页数：5

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