1gc1
HIV-1 GP120 CORE COMPLEXED WITH CD4 AND A NEUTRALIZING HUMAN ANTIBODY
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OverviewOverview
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.
About this StructureAbout this Structure
1GC1 is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 1 with NAG as ligand. Structure known Active Site: O. Full crystallographic information is available from OCA.
ReferenceReference
Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody., Kwong PD, Wyatt R, Robinson J, Sweet RW, Sodroski J, Hendrickson WA, Nature. 1998 Jun 18;393(6686):648-59. PMID:9641677
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