2B0S

Crystal structure analysis of anti-HIV-1 V3 Fab 2219 in complex with MN peptide

Summary for 2B0S

• Entry DOI: 10.2210/pdb2b0s/pdb
• Related: 2B1A 2B1H
• Descriptor: Fab 2219, light chain, Fab 2219, heavy chain, MN peptide of Exterior membrane glycoprotein GP120, ... (6 entities in total)
• Functional Keywords: fab-peptide complex; hiv-1; gp120; v3 loop, immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 49630.94

Authors

Stanfield, R.L.,Gorny, M.K.,Zolla-Pazner, S.,Wilson, I.A. (deposition date: 2005-09-14, release date: 2006-07-04, Last modification date: 2024-10-30)

Primary citation

Stanfield, R.L.,Gorny, M.K.,Zolla-Pazner, S.,Wilson, I.A.
Crystal structures of human immunodeficiency virus type 1 (HIV-1) neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity.
J.Virol., 80:6093-6105, 2006

PubMed Abstract: Human monoclonal antibody 2219 is a neutralizing antibody isolated from a human immunodeficiency virus type 1-infected individual. 2219 was originally selected for binding to a V3 fusion protein and can neutralize primary isolates from subtypes B, A, and F. Thus, 2219 represents a cross-reactive, human anti-V3 antibody. Fab 2219 binds to one face of the variable V3 beta-hairpin, primarily contacting conserved residues on the N-terminal beta-strand of V3, leaving the V3 crown or tip largely accessible. Three V3/2219 complexes reveal the antibody-bound conformations for both the N- and C-terminal regions that flank the V3 crown and illustrate how twisting of the V3 loop alters the relative dispositions and pairing of the amino acids in the adjacent V3 beta-strands and how the antibody can accommodate V3 loops with different sequences.

PubMed: 16731948
DOI: 10.1128/JVI.00205-06

Experimental method

X-RAY DIFFRACTION (2.3 Å)