3MLW

Crystal structure of anti-HIV-1 V3 Fab 1006-15D in complex with an MN V3 peptide

Summary for 3MLW

• Entry DOI: 10.2210/pdb3mlw/pdb
• Related: 3MLR 3MLS 3MLT 3MLU 3MLV 3MLX 3MLY 3MLZ
• Descriptor: Human monoclonal anti-HIV-1 gp120 V3 antibody 1006-15D Fab light chain, Human monoclonal anti-HIV-1 gp120 V3 antibody 1006-15D Fab heavy chain, HIV-1 gp120 third variable region (V3) crown, ... (5 entities in total)
• Functional Keywords: human monoclonal antibody, fab, hiv-1, gp120, third variable loop, antibody-antigen interaction, immune system
• Biological source: Homo sapiens; More
• Cellular location: Surface protein gp120: Virion membrane ; Peripheral membrane protein . Transmembrane protein gp41: Virion membrane ; Single-pass type I membrane protein : P05877
• Total number of polymer chains: 6
• Total formula weight: 101211.91

Authors

Kong, X.-P. (deposition date: 2010-04-18, release date: 2010-07-14, Last modification date: 2017-11-08)

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 (2.7 Å)