1BOG

ANTI-P24 (HIV-1) FAB FRAGMENT CB41 COMPLEXED WITH AN EPITOPE-HOMOLOGOUS PEPTIDE

Summary for 1BOG

• Entry DOI: 10.2210/pdb1bog/pdb
• Descriptor: ANTIBODY (CB 4-1), PEPTIDE, ... (4 entities in total)
• Functional Keywords: polyspecificity, cross reactivity, fab-fragment, hiv-1, complex (antibody-peptide), complex (antibody-peptide) complex, complex (antibody/peptide)
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 3
• Total formula weight: 47828.57

Authors

Keitel, T.,Kramer, A.,Wessner, H.,Scholz, C.,Schneider-Mergener, J.,Hoehne, W. (deposition date: 1998-08-04, release date: 1999-03-23, Last modification date: 2024-10-23)

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

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: 9413990
DOI: 10.1016/S0092-8674(00)80469-9

Experimental method

X-RAY DIFFRACTION (2.6 Å)