1ICE

STRUCTURE AND MECHANISM OF INTERLEUKIN-1BETA CONVERTING ENZYME

1ICE の概要

• エントリーDOI: 10.2210/pdb1ice/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000252
• 分子名称: INTERLEUKIN-1 BETA CONVERTING ENZYME, TETRAPEPTIDE ALDEHYDE, ... (4 entities in total)
• 機能のキーワード: cytokine, 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: P29466 P29466
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 29546.00

構造登録者

Wilson, K.P.,Griffith, J.P.,Kim, E.E.,Navia, M.A. (登録日: 1994-09-29, 公開日: 1995-07-28, 最終更新日: 2024-10-23)

主引用文献

Wilson, K.P.,Black, J.A.,Thomson, J.A.,Kim, E.E.,Griffith, J.P.,Navia, M.A.,Murcko, M.A.,Chambers, S.P.,Aldape, R.A.,Raybuck, S.A.
Structure and mechanism of interleukin-1 beta converting enzyme.
Nature, 370:270-275, 1994

PubMed Abstract: Interleukin-1 beta converting enzyme (ICE) processes an inactive precursor to the proinflammatory cytokine, interleukin-1 beta, and may regulate programmed cell death in neuronal cells. The high-resolution structure of human ICE in complex with an inhibitor has been determined by X-ray diffraction. The structure confirms the relationship between human ICE and cell-death proteins in other organisms. The active site spans both the 10 and 20K subunits, which associate to form a tetramer, suggesting a mechanism for ICE autoactivation.

PubMed: 8035875
DOI: 10.1038/370270a0

実験手法

X-RAY DIFFRACTION (2.6 Å)