Crystal structure of a fully glycosylated HIV-1 gp120 core reveals a stabilizing role for the glycan at Asn262
Crystal structure of a fully glycosylated HIV-1 gp120 core reveals a stabilizing role for the glycan at Asn262
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DOI：
10.1002/prot.24747
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发表时间：
2015-03-01
影响因子：
2.9
通讯作者：
Kwong, Peter D.
中科院分区：
文献类型：
--
作者：
Kong, Leopold;Wilson, Ian A.;Kwong, Peter D.
完全糖基化的HIV-1 gp120核心与CD4受体和Fab 17b形成复合体，在4.5埃分辨率下的晶体结构表明，核心gp120的15个N连接的糖链中有9个是部分有序的。Asn262位的多糖具有最广泛和有序的电子密度，并模拟了GlcNAc(2)Man(7)。这种多糖的GlcNAc茎大部分埋在gp120的裂隙中，这表明它在gp120的折叠和稳定性中发挥了作用。它的手臂与来自寡聚糖膜的邻近糖链的茎相互作用，寡聚糖膜是广泛中和抗体的主要靶点。蛋白质2015；83：590-596。(C)2014年威利期刊公司。
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.