Structure of a V3-Containing HIV-1 gp120 Core
| Autor: | Shahzad Majeed, Robyn L. Stanfield, Dimiter S. Dimitrov, Mei-Yun Zhang, Richard T. Wyatt, Elizabeth A. Montabana, Min Tang, Bette T. Korber, Ian A. Wilson, Peter D. Kwong, Joseph Sodroski, Chih-chin Huang |
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| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular Receptors CXCR4 Receptors CCR5 Protein Conformation viruses Molecular Sequence Data Context (language use) Plasma protein binding Immunodominance HIV Antibodies HIV Envelope Protein gp120 Biology V3 loop Crystallography X-Ray Article Protein structure Humans Amino Acid Sequence Binding site Peptide sequence chemistry.chemical_classification Binding Sites Multidisciplinary Immunodominant Epitopes virus diseases Hydrogen Bonding Molecular biology Peptide Fragments Protein Structure Tertiary chemistry CD4 Antigens HIV-1 Biophysics Crystallization Glycoprotein Protein Binding |
| Zdroj: | Science. 310:1025-1028 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.1118398 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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