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2NY2

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

Summary for 2NY2
Entry DOI10.2210/pdb2ny2/pdb
Related1GC1 1RZJ 1RZK 2NXY 2NXZ 2NY0 2NY1 2NY3 2NY4 2NY5 2NY6 2NY7
Related PRD IDPRD_900003
DescriptorENVELOPE GLYCOPROTEIN GP120, T-cell surface glycoprotein CD4, ANTIBODY 17B, LIGHT CHAIN, ... (9 entities in total)
Functional Keywordshiv, gp120, antibody, cd4, viral protein-immune system complex, viral protein/immune system
Biological sourceHuman immunodeficiency virus 1
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Total number of polymer chains4
Total formula weight106468.35
Authors
Primary citationZhou, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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