期刊
SCIENCE
卷 310, 期 5750, 页码 1025-1028出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1118398
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资金
- Intramural NIH HHS [Z99 AI999999] Funding Source: Medline
- NIAID NIH HHS [AI40895, AI31783, AI39429, AI24755] Funding Source: Medline
- NIGMS NIH HHS [GM46192] Funding Source: Medline
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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