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
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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