1q1j
From Proteopedia
Crystal Structure Analysis of anti-HIV-1 Fab 447-52D in complex with V3 peptide
Overview
447-52D is a human monoclonal antibody isolated from a heterohybridoma derived from an HIV-1-infected individual. This antibody recognizes the hypervariable gp120 V3 loop, and neutralizes both X4 and R5 primary isolates, making it one of the most effective anti-V3 antibodies characterized to date. The crystal structure of the 447-52D Fab in complex with a 16-mer V3 peptide at 2.5 A resolution reveals that the peptide beta hairpin forms a three-stranded mixed beta sheet with complementarity determining region (CDR) H3, with most of the V3 side chains exposed to solvent. Sequence specificity is conferred through interaction of the type-II turn (residues GPGR) at the apex of the V3 hairpin with the base of CDR H3. This novel mode of peptide-antibody recognition enables the antibody to bind to many different V3 sequences where only the GPxR core epitope is absolutely required.
About this Structure
Full crystallographic information is available from OCA.
Reference
Structural rationale for the broad neutralization of HIV-1 by human monoclonal antibody 447-52D., Stanfield RL, Gorny MK, Williams C, Zolla-Pazner S, Wilson IA, Structure. 2004 Feb;12(2):193-204. PMID:14962380 Page seeded by OCA on Sat May 3 05:45:09 2008
