2NY2

HIV-1 gp120 Envelope Glycoprotein (T123C, T257S, S334A, S375W, G431C) Complexed with CD4 and Antibody 17b

Summary for 2NY2

• Entry DOI: 10.2210/pdb2ny2/pdb
• Related: 1GC1 1RZJ 1RZK 2NXY 2NXZ 2NY0 2NY1 2NY3 2NY4 2NY5 2NY6 2NY7
• Related PRD ID: PRD_900003
• Descriptor: ENVELOPE GLYCOPROTEIN GP120, T-cell surface glycoprotein CD4, ANTIBODY 17B, LIGHT CHAIN, ... (9 entities in total)
• Functional Keywords: hiv, gp120, antibody, cd4, viral protein-immune system complex, viral protein/immune system
• Biological source: Human immunodeficiency virus 1; More
• Total number of polymer chains: 4
• Total formula weight: 106468.35

Authors

Zhou, T.,Xu, L.,Dey, B.,Hessell, A.J.,Van Ryk, D.,Xiang, S.H.,Yang, X.,Zhang, M.Y.,Zwick, M.B.,Arthos, J.,Burton, D.R.,Dimitrov, D.S.,Sodroski, J.,Wyatt, R.,Nabel, G.J.,Kwong, P.D. (deposition date: 2006-11-20, release date: 2007-02-06, Last modification date: 2024-11-06)

Primary citation

Zhou, T.,Xu, L.,Dey, B.,Hessell, A.J.,Van Ryk, D.,Xiang, S.H.,Yang, X.,Zhang, M.Y.,Zwick, M.B.,Arthos, J.,Burton, D.R.,Dimitrov, D.S.,Sodroski, J.,Wyatt, R.,Nabel, G.J.,Kwong, P.D.
Structural definition of a conserved neutralization epitope on HIV-1 gp120.
Nature, 445:732-737, 2007

PubMed 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.

PubMed: 17301785
DOI: 10.1038/nature05580

Experimental method

X-RAY DIFFRACTION (2 Å)