3GO1

Crystal structure of anti-HIV-1 Fab 268-D in complex with V3 peptide MN

Summary for 3GO1

• Entry DOI: 10.2210/pdb3go1/pdb
• Descriptor: Fab 268-D, light chain, Fab 268-D, heavy chain, Envelope glycoprotein gp160, ... (5 entities in total)
• Functional Keywords: hiv, v3 loop, antibody-antigen interactions, aids, apoptosis, cell membrane, cleavage on pair of basic residues, disulfide bond, envelope protein, fusion protein, glycoprotein, host-virus interaction, membrane, transmembrane, viral immunoevasion, virion, immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 48192.58

Authors

Kong, X.P.,Burke, V.J. (deposition date: 2009-03-18, release date: 2010-06-23, Last modification date: 2024-11-06)

Primary citation

Jiang, X.,Burke, V.,Totrov, M.,Williams, C.,Cardozo, T.,Gorny, M.K.,Zolla-Pazner, S.,Kong, X.P.
Conserved structural elements in the V3 crown of HIV-1 gp120.
Nat.Struct.Mol.Biol., 17:955-961, 2010

PubMed Abstract: Binding of the third variable region (V3) of the HIV-1 envelope glycoprotein gp120 to the cell-surface coreceptors CCR5 or CXCR4 during viral entry suggests that there are conserved structural elements in this sequence-variable region. These conserved elements could serve as epitopes to be targeted by a vaccine against HIV-1. Here we perform a systematic structural analysis of representative human anti-V3 monoclonal antibodies in complex with V3 peptides, revealing that the crown of V3 has four conserved structural elements: an arch, a band, a hydrophobic core and the peptide backbone. These are either unaffected by or are subject to minimal sequence variation. As these regions are targeted by cross-clade neutralizing human antibodies, they provide a blueprint for the design of vaccine immunogens that could elicit broadly cross-reactive protective antibodies.

PubMed: 20622876
DOI: 10.1038/nsmb.1861

Experimental method

X-RAY DIFFRACTION (1.89 Å)