2NY3: Hiv-1 Gp120 Envelope Glycoprotein (k231c, T257s, E267c, S334a, S375w) Complexed With Cd4 And Antibody 17b

Citation:
Abstract
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.
PDB ID: 2NY3Download
MMDB ID: 44084
PDB Deposition Date: 2006/11/20
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Human immunodeficiency virus 1
Similar Structures:
Biological Unit for 2NY3: tetrameric; determined by author
Molecular Components in 2NY3
Label Count Molecule
Proteins (4 molecules)
1
Envelope Glycoprotein Gp120
Molecule annotation
1
T-cell Surface Glycoprotein CD4(Gene symbol: CD4)
Molecule annotation
1
Antibody 17b, Light Chain
Molecule annotation
1
Antibody 17b, Heavy Chain
Molecule annotation
Chemicals (14 molecules)
1
13
2
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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