1PAU

Crystal structure of the complex of apopain with the tetrapeptide aldehyde inhibitor AC-DEVD-CHO

1PAU の概要

• エントリーDOI: 10.2210/pdb1pau/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000422
• 分子名称: APOPAIN, ACE-ASP-GLU-VAL-ASJ, ... (4 entities in total)
• 機能のキーワード: cysteine protease, caspase-3, apopain, cpp32, yama, protease-inhibitor complex, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P42574 P42574
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 29038.99

構造登録者

Rotonda, J.,Becker, J.W. (登録日: 1996-06-06, 公開日: 1997-07-07, 最終更新日: 2023-08-09)

主引用文献

Rotonda, J.,Nicholson, D.W.,Fazil, K.M.,Gallant, M.,Gareau, Y.,Labelle, M.,Peterson, E.P.,Rasper, D.M.,Ruel, R.,Vaillancourt, J.P.,Thornberry, N.A.,Becker, J.W.
The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis.
Nat.Struct.Biol., 3:619-625, 1996

PubMed Abstract: Cysteine proteases related to mammalian interleukin-1 beta converting enzyme (ICE) and to its Caenorhabditis elegans homologue, CED-3, play a critical role in the biochemical events that culminate in apoptosis. We have determined the three-dimensional structure of a complex of the human CED-3 homologue CPP32/apopain with a potent tetrapeptide-aldehyde inhibitor. The protein resembles ICE in overall structure, but its S4 subsite is strikingly different in size and chemical composition. These differences account for the variation in specificity between the ICE- and CED-3-related proteases and enable the design of specific inhibitors that can probe the physiological functions of the proteins and disease states with which they are associated.

PubMed: 8673606
DOI: 10.1038/nsb0796-619

実験手法

X-RAY DIFFRACTION (2.5 Å)