Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1998-06

AUTHORS

Peter D. Kwong, Richard Wyatt, James Robinson, Raymond W. Sweet, Joseph Sodroski, Wayne A. Hendrickson

ABSTRACT

The entry of human immunodeficiency virus (HIV) into cells requires the sequential interaction of the viral exterior envelope glycoprotein, gp120, with the CD4 glycoprotein and a chemokine receptor on the cell surface. These interactions initiate a fusion of the viral and cellular membranes. Although gp120 can elicit virus-neutralizing antibodies, HIV eludes the immune system. We have solved the X-ray crystal structure at 2.5 A resolution of an HIV-1 gp120 core complexed with a two-domain fragment of human CD4 and an antigen-binding fragment of a neutralizing antibody that blocks chemokine-receptor binding. The structure reveals a cavity-laden CD4-gp120 interface, a conserved binding site for the chemokine receptor, evidence for a conformational change upon CD4 binding, the nature of a CD4-induced antibody epitope, and specific mechanisms for immune evasion. Our results provide a framework for understanding the complex biology of HIV entry into cells and should guide efforts to intervene. More... »

PAGES

648

Journal

TITLE

Nature

ISSUE

6686

VOLUME

393

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/31405

    DOI

    http://dx.doi.org/10.1038/31405

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1038246480

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/9641677


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