Crystal structure of a fully glycosylated HIV-1 gp120 core reveals a stabilizing role for the glycan at Asn262

被引：40

作者：

Kong, Leopold ^{[1
,2
,3
,4
,5
]}

Wilson, Ian A. ^{[2
,3
,4
,5
,6
]}

Kwong, Peter D. ^{[1
]}

机构：

[1] NIH, Vaccine Res Ctr, Bethesda, MD 20892 USA

[2] Scripps Res Inst, Dept Integrat Struct & Computat Biol, La Jolla, CA 92037 USA

[3] Scripps Res Inst, Int AIDS Vaccine Initiat Neutralizing Antibody Ct, La Jolla, CA 92037 USA

[4] Scripps Res Inst, Collaborat AIDS Vaccine Discovery, La Jolla, CA 92037 USA

[5] Scripps Res Inst, Scripps Ctr HIV AIDS Vaccine Immunol & Immunogen, La Jolla, CA 92037 USA

[6] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2015年 / 83卷 / 03期

关键词：

HIV-1; gp120; glycan shield; role of N262; NEUTRALIZING ANTIBODIES; ENVELOPE GLYCOPROTEIN; TARGET; TRIMER; BROAD;

D O I：

10.1002/prot.24747

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：

The crystal structure of a fully glycosylated HIV-1 gp120 core in complex with CD4 receptor and Fab 17b at 4.5-angstrom resolution reveals 9 of the 15 N-linked glycans of core gp120 to be partially ordered. The glycan at position Asn262 had the most extensive and well-ordered electron density, and a GlcNAc(2)Man(7) was modeled. The GlcNAc stem of this glycan is largely buried in a cleft in gp120, suggesting a role in gp120 folding and stability. Its arms interact with the stems of neighboring glycans from the oligomannose patch, which is a major target for broadly neutralizing antibodies. Proteins 2015; 83:590-596. (c) 2014 Wiley Periodicals, Inc.

引用

收藏

页码：590 / 596

页数：7

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