Binding of full-length HIV-1 gp120 to CD4 induces structural reorientation around the gp120 core

被引：8

作者：

Ashish

Garg, Renu

Anguita, Juan

Krueger, Joanna K. ^{[1
]}

机构：

[1] Univ N Carolina, Dept Chem, Charlotte, NC 28213 USA

[2] Univ N Carolina, Dept Biol, Charlotte, NC 28213 USA

[3] Univ Massachusetts, Dept Vet & Anim Sci, Amherst, MA 01003 USA

来源：

BIOPHYSICAL JOURNAL | 2006年 / 91卷 / 06期

关键词：

D O I：

10.1529/biophysj.106.090381

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Small-angle x-ray scattering data on the unliganded full-length fully glycosylated HIV-1 gp120, the soluble CD4 (domains 1-2) receptor, and their complex in solution are presented. Ab initio structure restorations using these data provides the first look at the envelope shape for the unliganded and the complexed gp 120 molecule. Fitting known crystal structures of the unliganded SIV and the complexed HIV gp 120 core regions within our resultant shape constraints reveals movement of the V3 loop upon binding.

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收藏

页码：L69 / L71

页数：3

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