2A2N

Crystal Structure of the peptidylprolyl isomerase domain of Human PPWD1

2A2N の概要

• エントリーDOI: 10.2210/pdb2a2n/pdb
• 分子名称: peptidylprolyl isomerase domain and WD repeat containing 1, GLYCEROL (3 entities in total)
• 機能のキーワード: cis-trans isomerization, protein-folding, peptidylprolyl isomerase, structural genomics, structural genomics consortium, sgc, isomerase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q96BP3
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 58585.90

構造登録者

Walker, J.R.,Davis, T.L.,Newman, E.M.,Mackenzie, F.,Sundstrom, M.,Arrowsmith, C.,Edwards, A.,Bochkarev, A.,Dhe-Paganon, S.,Structural Genomics Consortium (SGC) (登録日: 2005-06-22, 公開日: 2005-07-05, 最終更新日: 2023-08-23)

主引用文献

Davis, T.L.,Walker, J.R.,Ouyang, H.,MacKenzie, F.,Butler-Cole, C.,Newman, E.M.,Eisenmesser, E.Z.,Dhe-Paganon, S.
The crystal structure of human WD40 repeat-containing peptidylprolyl isomerase (PPWD1).
Febs J., 275:2283-2295, 2008

PubMed Abstract: Cyclophilins comprise one of the three classes of peptidylprolyl isomerases found in all eukaryotic and prokaryotic organisms, as well as viruses. Many of the 17 annotated human cyclophilins contain the catalytic domain in tandem with other domains, and many of the specific functions of a particular cyclophilin or its associated domains remain unknown. The structure of the isomerase domain from a spliceosome-associated cyclophilin, PPWD1 (peptidylprolyl isomerase containing WD40 repeat), has been solved to 1.65 A. In the crystal, the N-terminus of one isomerase domain is bound in the active site of a neighboring isomerase molecule in a manner analogous to substrate. NMR solution studies show that this sequence binds to the active site of the cyclophilin, but cannot be turned over by the enzyme. A pseudo-substrate immediately N-terminal to the cyclophilin domain in PPWD1 could have wider implications for the function of this cyclophilin in the spliceosome, where it is located in human cells.

PubMed: 18397323
DOI: 10.1111/j.1742-4658.2008.06381.x

実験手法

X-RAY DIFFRACTION (1.65 Å)