3E4C

Procaspase-1 zymogen domain crystal structure

3E4C の概要

• エントリーDOI: 10.2210/pdb3e4c/pdb
• 関連するPDBエントリー: 1RWX
• 分子名称: Caspase-1, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: zymogen, caspase-1, inflammasome, ice, caspase, il-1b, procaspase-1, procaspase, innate immunity, apoptosis, hydrolase, protease, thiol protease
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67619.11

構造登録者

Elliott, J.M.,Rouge, L.,Wiesmann, C.,Scheer, J.M. (登録日: 2008-08-11, 公開日: 2008-12-30, 最終更新日: 2023-08-30)

主引用文献

Elliott, J.M.,Rouge, L.,Wiesmann, C.,Scheer, J.M.
Crystal structure of procaspase-1 zymogen domain reveals insight into inflammatory caspase autoactivation
J.Biol.Chem., 284:6546-6553, 2009

PubMed Abstract: One key event in inflammatory signaling is the activation of the initiator caspase, procaspase-1. Presented here is the crystal structure of the procaspase-1 zymogen without its caspase recruitment domain solved to 2.05 A. Although the isolated domain is monomeric in solution, the protein appeared dimeric in crystals. The loop arrangements in the dimer provide insight into the first autoproteolytic events that occur during activation by oligomerization. Additionally, in contrast to other caspases, we demonstrate that autoproteolysis at the second cleavage site, Asp316, is necessary for conversion to a stable dimer in solution. Critical elements of secondary structure are revealed in the crystal structure that explain why a dimeric protein is favored after proteolysis at this aspartic acid. Dimer stabilization is concurrent with a 130-fold increase in kcat, the sole contributing kinetic factor to an activated and efficient mediator of inflammation.

PubMed: 19117953
DOI: 10.1074/jbc.M806121200

実験手法

X-RAY DIFFRACTION (2.05 Å)