3SIP

Crystal structure of drICE and dIAP1-BIR1 complex

3SIP の概要

• エントリーDOI: 10.2210/pdb3sip/pdb
• 関連するPDBエントリー: 3SIQ
• 分子名称: Caspase, Apoptosis 1 inhibitor, ZINC ION, ... (4 entities in total)
• 機能のキーワード: caspase, bir domain, hydrolase-ligase-hydrolase complex, hydrolase/ligase/hydrolase
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 87403.62

構造登録者

Li, X.,Wang, J.,Shi, Y. (登録日: 2011-06-20, 公開日: 2011-08-10, 最終更新日: 2023-11-01)

主引用文献

Li, X.,Wang, J.,Shi, Y.
Structural mechanisms of DIAP1 auto-inhibition and DIAP1-mediated inhibition of drICE.
Nat Commun, 2:408-408, 2011

PubMed Abstract: The Drosophila inhibitor of apoptosis protein DIAP1 exists in an auto-inhibited conformation, unable to suppress the effector caspase drICE. Auto-inhibition is disabled by caspase-mediated cleavage of DIAP1 after Asp20. The cleaved DIAP1 binds to mature drICE, inhibits its protease activity, and, presumably, also targets drICE for ubiquitylation. DIAP1-mediated suppression of drICE is effectively antagonized by the pro-apoptotic proteins Reaper, Hid, and Grim (RHG). Despite rigorous effort, the molecular mechanisms behind these observations are enigmatic. Here we report a 2.4 Å crystal structure of uncleaved DIAP1-BIR1, which reveals how the amino-terminal sequences recognize a conserved surface groove in BIR1 to achieve auto-inhibition, and a 3.5 Å crystal structure of active drICE bound to cleaved DIAP1-BIR1, which provides a structural explanation to DIAP1-mediated inhibition of drICE. These structures and associated biochemical analyses, together with published reports, define the molecular determinants that govern the interplay among DIAP1, drICE and the RHG proteins.

PubMed: 21811237
DOI: 10.1038/ncomms1418

実験手法

X-RAY DIFFRACTION (3.496 Å)