Cyanovirin-N: a sugar-binding antiviral protein with a new twist

被引：51

作者：

Botos, I ^{[1
]}

Wlodawer, A ^{[1
]}

机构：

[1] Natl Canc Inst, MCL, Frederick, MD 21702 USA

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 2003年 / 60卷 / 02期

关键词：

cyanovirin-N; anti-HIV activity; 3D domain-swapping; gp120; protein folding; X-ray; NMR;

D O I：

10.1007/s000180300023

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：

Cyanovirin-N (CV-N), an 11-kDa protein from the cyanobacterium Nostoc ellipsosporum, is a highly potent virucidal agent that has generated interest as a lead natural product for the prevention and chemotherapy of human immunodeficiency virus infection. The antiviral activity of CV-N is mediated through specific, high-affinity interactions with the viral surface envelope glycoproteins. A number of structures of wild-type, mutant and sequence-shuffled CV-N have been solved by nuclear magnetic resonance and crystallography, showing that the protein exists as either a quasi-symmetric two-domain monomer or a domain-swapped dimer. Structures of several complexes of CV-N with oligosaccharides help in explaining the unique mode of high-affinity binding of these molecules to both forms of CV-N.

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页码：277 / 287

页数：11

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