3OD5

Crystal structure of active caspase-6 bound with Ac-VEID-CHO

3OD5 の概要

• エントリーDOI: 10.2210/pdb3od5/pdb
• 関連するPDBエントリー: 3NR2
• 関連するBIRD辞書のPRD_ID: PRD_000976
• 分子名称: Caspase-6, peptide aldehyde inhibitor AC-VEID-CHO, CACODYLATE ION, ... (4 entities in total)
• 機能のキーワード: caspase domain, apoptotic protease, 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: P55212
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 66174.27

構造登録者

Wang, X.-J.,Liu, X.,Wang, K.-T.,Cao, Q.,Su, X.-D. (登録日: 2010-08-11, 公開日: 2010-10-27, 最終更新日: 2024-11-13)

主引用文献

Wang, X.-J.,Cao, Q.,Liu, X.,Wang, K.-T.,Mi, W.,Zhang, Y.,Li, L.-F.,Leblanc, A.C.,Su, X.-D.
Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation
Embo Rep., 11:841-847, 2010

PubMed Abstract: Dimeric effectors caspase 3 and caspase 7 are activated by initiator caspase processing. In this study, we report the crystal structures of effector caspase 6 (CASP6) zymogen and N-Acetyl-Val-Glu-Ile-Asp-al-inhibited CASP6. Both of these forms of CASP6 have a dimeric structure, and in CASP6 zymogen the intersubunit cleavage site (190)TEVD(193) is well structured and inserts into the active site. This positions residue Asp 193 to be easily attacked by the catalytic residue Cys 163. We demonstrate biochemically that intramolecular cleavage at Asp 193 is a prerequisite for CASP6 self-activation and that this activation mechanism is dependent on the length of the L2 loop. Our results indicate that CASP6 can be activated and regulated through intramolecular self-cleavage.

PubMed: 20890311
DOI: 10.1038/embor.2010.141

実験手法

X-RAY DIFFRACTION (1.6 Å)