Epitopes described in "Structure of a V3-containing HIV-1 gp120 core."

Article Authors:Chih-chin Huang; Min Tang; Mei-Yun Zhang; Shahzad Majeed; Elizabeth Montabana; Robyn L Stanfield; Dimiter S Dimitrov; Bette Korber; Joseph Sodroski; Ian A Wilson; Richard Wyatt; Peter D Kwong
Article Title:Structure of a V3-containing HIV-1 gp120 core.
Reference Detail
Reference ID:1022134
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.
Affiliations:Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892, USA.
Reference Type:Literature
PubMed ID:16284180
Journal Volume:310
Article Pages:1025-8
Journal ISSN:1095-9203
Article Chemical List:Antigens, CD4;HIV Antibodies;HIV Envelope Protein gp120;HIV envelope protein gp120 (305-321);Immunodominant Epitopes;Peptide Fragments;Receptors, CCR5;Receptors, CXCR4
Article MeSH List:Amino Acid Sequence; Antigens, CD4(chemistry; metabolism); Binding Sites; Crystallization; Crystallography, X-Ray; HIV Antibodies(immunology); HIV Envelope Protein gp120(chemistry; immunology; metabolism); HIV-1(chemistry; immunology; metabolism); Humans; Hydrogen Bonding; Immunodominant Epitopes; Models, Molecular; Molecular Sequence Data; Peptide Fragments(chemistry; immunology; metabolism); Protein Binding; Protein Conformation; Protein Structure, Tertiary; Receptors, CCR5(chemistry; metabolism); Receptors, CXCR4(chemistry; metabolism)
Curation Last Updated:2015-06-05 02:43:50