1CFS
ANTI-P24 (HIV-1) FAB FRAGMENT CB41 COMPLEXED WITH AN EPITOPE-UNRELATED PEPTIDE
Summary for 1CFS
| Entry DOI | 10.2210/pdb1cfs/pdb |
| Descriptor | PROTEIN (IGG2A KAPPA ANTIBODY CB41 (LIGHT CHAIN)), PROTEIN (IGG2A KAPPA ANTIBODY CB41 (HEAVY CHAIN)), PROTEIN (ANTIGEN BOUND PEPTIDE), ... (4 entities in total) |
| Functional Keywords | polyspecificity, cross reactivity, fab-fragment, hiv-1 |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 3 |
| Total formula weight | 47821.59 |
| Authors | Keitel, T.,Kramer, A.,Wessner, H.,Scholz, C.,Schneider-Mergener, J.,Hoehne, W. (deposition date: 1999-03-19, release date: 1999-03-31, Last modification date: 2023-12-27) |
| Primary citation | Keitel, T.,Kramer, A.,Wessner, H.,Scholz, C.,Schneider-Mergener, J.,Hohne, W. Crystallographic analysis of anti-p24 (HIV-1) monoclonal antibody cross-reactivity and polyspecificity. Cell(Cambridge,Mass.), 91:811-820, 1997 Cited by PubMed Abstract: The X-ray crystal structures of an anti-p24 (HIV-1) monoclonal antibody Fab fragment alone and in complexes with the epitope peptide GATPQDLNTnL (n = norleucine), an epitope-homologous peptide GATPEDLNQKLAGN, as well as two unrelated peptides GLYEWGGARITNTD and efslkGpllqwrsG (D-peptide), are presented to a maximum resolution of 2.6 A. The latter three peptides were identified from screening synthetic combinatorial peptide libraries. Although all peptides bind to the same antigen combining site, the nonhomologous peptides adopt different binding conformations and also form their critical contacts with different antibody residues. Only small readjustments are observed within the framework of the Fab fragment upon binding. PubMed: 9413990DOI: 10.1016/S0092-8674(00)80469-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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