2b1a
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(New page: 200px<br /> <applet load="2b1a" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b1a, resolution 2.348Å" /> '''Crystal structure ...)
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Revision as of 12:36, 8 November 2007
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Crystal structure analysis of anti-HIV-1 V3 Fab 2219 in complex with UG1033 peptide
Overview
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.
About this Structure
2B1A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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., Stanfield RL, Gorny MK, Zolla-Pazner S, Wilson IA, J Virol. 2006 Jun;80(12):6093-105. PMID:16731948
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