1Q1J
Crystal Structure Analysis of anti-HIV-1 Fab 447-52D in complex with V3 peptide
Summary for 1Q1J
| Entry DOI | 10.2210/pdb1q1j/pdb |
| Descriptor | Fab 447-52D, light chain, Fab 447-52D, heavy chain, gp120 V3 peptide, ... (4 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 | 6 |
| Total formula weight | 98550.14 |
| Authors | Stanfield, R.L.,Gorny, M.K.,Williams, C.,Zolla-Pazner, S.,Wilson, I.A. (deposition date: 2003-07-21, release date: 2004-02-17, Last modification date: 2024-11-06) |
| Primary citation | Stanfield, R.L.,Gorny, M.K.,Williams, C.,Zolla-Pazner, S.,Wilson, I.A. Structural rationale for the broad neutralization of HIV-1 by human monoclonal antibody 447-52D. Structure, 12:193-204, 2004 Cited by PubMed Abstract: 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. PubMed: 14962380DOI: 10.1016/j.str.2004.01.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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