Structure of a V3-Containing HIV-1 gp120 Core-Reference-Cited by-同舟云学术

Structure of a V3-Containing HIV-1 gp120 Core

Published:2005-11-11 Issue:5750 Volume:310 Page:1025-1028
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Huang Chih-chin¹²³⁴⁵,Tang Min¹²³⁴⁵,Zhang Mei-Yun¹²³⁴⁵,Majeed Shahzad¹²³⁴⁵,Montabana Elizabeth¹²³⁴⁵,Stanfield Robyn L.¹²³⁴⁵,Dimitrov Dimiter S.¹²³⁴⁵,Korber Bette¹²³⁴⁵,Sodroski Joseph¹²³⁴⁵,Wilson Ian A.¹²³⁴⁵,Wyatt Richard¹²³⁴⁵,Kwong Peter D.¹²³⁴⁵

Affiliation:

1. Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892, USA.

2. Basic Research Program, SAIC-Frederick, Center for Cancer Research Nanobiology Program, National Cancer Institute, Frederick, MD 21702, USA.

3. Protein Interaction Group, Center for Cancer Research Nanobiology Program, National Cancer Institute, Frederick, MD 21702, USA.

4. Department of Molecular Biology and Skaggs Institute for Chemical Biology, Scripps Research Institute, La Jolla, CA 92037, USA.

5. Theoretical Biology (T10), Los Alamos National Laboratory, Los Alamos, NM 87545, USA.

Abstract

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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