2ny2: Difference between revisions
New page: left|200px<br /> <applet load="2ny2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ny2, resolution 2.00Å" /> '''HIV-1 gp120 Envelop... |
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Revision as of 23:57, 12 November 2007
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HIV-1 gp120 Envelope Glycoprotein (T123C, T257S, S334A, S375W, G431C) Complexed with CD4 and Antibody 17b
OverviewOverview
The remarkable diversity, glycosylation and conformational flexibility of, the human immunodeficiency virus type 1 (HIV-1) envelope (Env), including, substantial rearrangement of the gp120 glycoprotein upon binding the CD4, receptor, allow it to evade antibody-mediated neutralization. Despite this, complexity, the HIV-1 Env must retain conserved determinants that mediate, CD4 binding. To evaluate how these determinants might provide, opportunities for antibody recognition, we created variants of gp120, stabilized in the CD4-bound state, assessed binding of CD4 and of, receptor-binding-site antibodies, and determined the structure at 2.3 A, resolution of the broadly neutralizing antibody b12 in complex with gp120., b12 binds to a conformationally invariant surface that overlaps a distinct, subset of the CD4-binding site. This surface is involved in the metastable, attachment of CD4, before the gp120 rearrangement required for stable, engagement. A site of vulnerability, related to a functional requirement, for efficient association with CD4, can therefore be targeted by antibody, to neutralize HIV-1.
About this StructureAbout this Structure
2NY2 is a Single protein structure of sequence from Homo sapiens and Human immunodeficiency virus 1 with NAG, SUC, EDO and HEZ as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structural definition of a conserved neutralization epitope on HIV-1 gp120., Zhou T, Xu L, Dey B, Hessell AJ, Van Ryk D, Xiang SH, Yang X, Zhang MY, Zwick MB, Arthos J, Burton DR, Dimitrov DS, Sodroski J, Wyatt R, Nabel GJ, Kwong PD, Nature. 2007 Feb 15;445(7129):732-7. PMID:17301785
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