Structure of a V3-containing HIV-1 gp120 core

被引：605

作者：

Huang, CC

Tang, M

Zhang, MY

Majeed, S

Montabana, E

Stanfield, RL

Dimitrov, DS

Korber, B

Sodroski, J

Wilson, IA

Wyatt, R ^{[1
]}

Kwong, PD

机构：

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

[2] SAIC Frederick, Basic Res Program, Frederick, MD USA

[3] NCI, Prot Interact Grp, Ctr Canc Res, Nanobiol Program, Frederick, MD 21702 USA

[4] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA

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

[6] Los Alamos Natl Lab, Los Alamos, NM 87545 USA

[7] Harvard Univ, Sch Med, Dana Farber Canc Inst, Dept Canc Immunol & AIDS, Boston, MA 02115 USA

来源：

SCIENCE | 2005年 / 310卷 / 5750期

关键词：

D O I：

10.1126/science.1118398

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The third variable region (V3) of the HIV-1 gp120 envelope glycoprotein is immunodominant and contains features essential for coreceptor binding. We determined the structure of V3 in the context of an HIV-1 gp120 core complexed to the CD4 receptor and to the X5 antibody at 3.5 angstrom resolution. Binding of gp120 to cell-surface CD4 would position V3 so that its coreceptor-binding tip protrudes 30 angstroms from the core toward the target cell membrane. The extended nature and antibody accessibility of V3 explain its immunodominance. Together, the results provide a structural rationale for the role of V3 in HIV entry and neutralization.

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页码：1025 / 1028

页数：4

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