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| [[Image:2ny7.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2ny7| PDB=2ny7 | SCENE= }} | | {{STRUCTURE_2ny7| PDB=2ny7 | SCENE= }} |
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| '''HIV-1 gp120 Envelope Glycoprotein Complexed with the Broadly Neutralizing CD4-Binding-Site Antibody b12'''
| | ===HIV-1 gp120 Envelope Glycoprotein Complexed with the Broadly Neutralizing CD4-Binding-Site Antibody b12=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_17301785}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17301785 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17301785}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Gp120]] | | [[Category: Gp120]] |
| [[Category: Hiv]] | | [[Category: Hiv]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:04:00 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:51:30 2008'' |
