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Structure of a V3-containing HIV-1 gp120 core

  1. Author:
    Huang, C. C.
    Tang, M.
    Zhang, M. Y.
    Majeed, S.
    Montabana, E.
    Stanfield, R. L.
    Dimitrov, D. S.
    Korber, B.
    Sodroski, J.
    Wilson, I. A.
    Wyatt, R.
    Kwong, P. D.

  2. Author Address

    NIAID, Vaccine Res Ctr, Bethesda, MD 20892 USA. SAIC Frederick, Basic Res Program, Frederick, MD USA. NCI, Prot Interact Grp, Ctr Canc Res, Nanobiol Program, Frederick, MD 21702 USA. Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA. Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA. Los Alamos Natl Lab, Los Alamos, NM 87545 USA. Harvard Univ, Sch Med, Dana Farber Canc Inst, Dept Canc Immunol & AIDS, Boston, MA 02115 USA Wyatt, R, NIAID, Vaccine Res Ctr, Bethesda, MD 20892 USA
    1. Year: 2005
    2. Date: NOV 11
  2. Journal: Science
    1. 310
    2. 5750
    3. Pages: 1025-1028
  4. Type of Article: Article
  1. 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

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External Sources

  1. View record in Web of Science®
  2. WOS: 000233343400046

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