1gc1: Difference between revisions

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[[Category: t-cell surface glycoprotein cd4]]
[[Category: t-cell surface glycoprotein cd4]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:22:44 2007''
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Revision as of 16:08, 30 October 2007

File:1gc1.gif


1gc1, resolution 2.5Å

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HIV-1 GP120 CORE COMPLEXED WITH CD4 AND A NEUTRALIZING HUMAN ANTIBODY

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 ... [(full description)]

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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OCA