1I3O

CRYSTAL STRUCTURE OF THE COMPLEX OF XIAP-BIR2 AND CASPASE 3

1I3O の概要

• エントリーDOI: 10.2210/pdb1i3o/pdb
• 関連するPDBエントリー: 1C9Q 1PAU
• 分子名称: CASPASE 3, BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 4, ZINC ION, ... (5 entities in total)
• 機能のキーワード: complex, iap, caspase, apoptosis
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P42574 P42574 P98170
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 93536.04

構造登録者

Riedl, S.J.,Renatus, M.,Schwarzenbacher, R.,Zhou, Q.,Sun, C.,Fesik, S.W.,Liddington, R.C.,Salvesen, G.S. (登録日: 2001-02-15, 公開日: 2001-03-21, 最終更新日: 2023-08-09)

主引用文献

Riedl, S.J.,Renatus, M.,Schwarzenbacher, R.,Zhou, Q.,Sun, C.,Fesik, S.W.,Liddington, R.C.,Salvesen, G.S.
Structural basis for the inhibition of caspase-3 by XIAP.
Cell(Cambridge,Mass.), 104:791-800, 2001

PubMed Abstract: The molecular mechanism(s) that regulate apoptosis by caspase inhibition remain poorly understood. The main endogenous inhibitors are members of the IAP family and are exemplified by XIAP, which regulates the initiator caspase-9, and the executioner caspases-3 and -7. We report the crystal structure of the second BIR domain of XIAP (BIR2) in complex with caspase-3, at a resolution of 2.7 A, revealing the structural basis for inhibition. The inhibitor makes limited contacts through its BIR domain to the surface of the enzyme, and most contacts to caspase-3 originate from the N-terminal extension. This lies across the substrate binding cleft, but in reverse orientation compared to substrate binding. The mechanism of inhibition is due to a steric blockade prohibitive of substrate binding, and is distinct from the mechanism utilized by synthetic substrate analog inhibitors.

PubMed: 11257232
DOI: 10.1016/S0092-8674(01)00274-4

実験手法

X-RAY DIFFRACTION (2.7 Å)