1CFS

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

1CFS の概要

• エントリーDOI: 10.2210/pdb1cfs/pdb
• 分子名称: PROTEIN (IGG2A KAPPA ANTIBODY CB41 (LIGHT CHAIN)), PROTEIN (IGG2A KAPPA ANTIBODY CB41 (HEAVY CHAIN)), PROTEIN (ANTIGEN BOUND PEPTIDE), ... (4 entities in total)
• 機能のキーワード: polyspecificity, cross reactivity, fab-fragment, hiv-1
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 47821.59

構造登録者

Keitel, T.,Kramer, A.,Wessner, H.,Scholz, C.,Schneider-Mergener, J.,Hoehne, W. (登録日: 1999-03-19, 公開日: 1999-03-31, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.75 Å)