1gc1

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(New page: 200px<br /> <applet load="1gc1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gc1, resolution 2.5&Aring;" /> '''HIV-1 GP120 CORE COM...)
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Revision as of 19:51, 29 October 2007


1gc1, resolution 2.5Å

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

Overview

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 Structure

1GC1 is a [Protein complex] structure of sequences from [Homo sapiens] and [Human immunodeficiency virus type 1] with NAG as [ligand]. Full crystallographic information is available from [OCA].

Reference

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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