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Structure of a V3-containing HIV-1 gp120 core.
Huang, Chih-chin; Tang, Min; Zhang, Mei-Yun; Majeed, Shahzad; Montabana, Elizabeth; Stanfield, Robyn L; Dimitrov, Dimiter S; Korber, Bette; Sodroski, Joseph; Wilson, Ian A; Wyatt, Richard; Kwong, Peter D.
Affiliation
  • Huang CC; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892, USA.
Science ; 310(5750): 1025-8, 2005 Nov 11.
Article in En | MEDLINE | ID: mdl-16284180
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.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peptide Fragments / CD4 Antigens / HIV Envelope Protein gp120 / HIV-1 Type of study: Prognostic_studies Limits: Humans Language: En Journal: Science Year: 2005 Document type: Article Affiliation country: Country of publication:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peptide Fragments / CD4 Antigens / HIV Envelope Protein gp120 / HIV-1 Type of study: Prognostic_studies Limits: Humans Language: En Journal: Science Year: 2005 Document type: Article Affiliation country: Country of publication: