Structure of an HIV-2 gp120 in Complex with CD4

被引：13
|
作者：
Davenport, Yunji W. [1 ,2 ]
West, Anthony P., Jr. [1 ]
Bjorkman, Pamela J. [1 ]
机构：
[1] CALTECH, Div Biol & Biol Engn, Pasadena, CA 91125 USA
[2] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA
来源：
JOURNAL OF VIROLOGY | 2016年 / 90卷 / 04期
关键词：
CRYSTAL-STRUCTURE; ANTIBODY; REFINEMENT; REVEALS; NEUTRALIZATION; EVOLUTION; FEATURES; EPITOPE; PHENIX; MODEL;
D O I：
10.1128/JVI.02678-15
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
HIV-2 is a nonpandemic form of the virus causing AIDS, and the majority of HIV-2-infected patients exhibit long-term nonprogression. The HIV-1 and HIV-2 envelope glycoproteins, the sole targets of neutralizing antibodies, share 30 to 40% identity. As a first step in understanding the reduced pathogenicity of HIV-2, we solved a 3.0-angstrom structure of an HIV-2 gp120 bound to the host receptor CD4, which reveals structural similarity to HIV-1 gp120 despite divergence in amino acid sequence.
引用
收藏
页码：2112 / 2118
页数：7
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