1W8V

Enzymatic and structural characterization of non peptide ligand cyclophilin complexes

1W8V の概要

• エントリーDOI: 10.2210/pdb1w8v/pdb
• 関連するPDBエントリー: 1W7Y 1W8L 1W8M
• 分子名称: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A (2 entities in total)
• 機能のキーワード: complex (isomerase-immunosuppressant), native high resolution, isomerase, multigene family, rotamase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18036.50

構造登録者

Kontopidis, G.,Taylor, P.,Walkinshaw, M. (登録日: 2004-09-28, 公開日: 2004-09-30, 最終更新日: 2023-12-13)

主引用文献

Kontopidis, G.,Taylor, P.,Walkinshaw, M.
Enzymatic and Structural Characterization of Non-Peptide Ligand-Cyclophilin Complexes
Acta Crystallogr.,Sect.D, 60:479-485, 2004

PubMed Abstract: Piperidine ligands are described that provide the first examples of non-peptidic ligand structures for the cyclophilin family of proteins. Crystal structures of two ligand complexes are compared with the unliganded protein and show ligand-induced changes in side-chain conformation and water binding. A peptidylprolyl cis-trans-isomerase assay showed the dissociation constants of the two ligands to be 320 and 25 mM. This study also provides the first published data for both enzymatic activity and three-dimensional structure for any protein-ligand complex that binds with a high-millimolar dissociation constant. The structures may be of relevance in the field of drug design, as they suggest starting points for the design of larger tighter-binding analogues.

PubMed: 14993672
DOI: 10.1107/S0907444904000174

実験手法

X-RAY DIFFRACTION (1.7 Å)