Crystal structure of RAIDD death domain implicates potential mechanism of PIDDosome assembly

JOURNAL OF MOLECULAR BIOLOGY

卷:357

Article

Park, HH ; Wu, H

关键词: crystal structure;    death domain;    apoptosis;    RAIDD;    PIDDosome;   

DOI  :  10.1016/j.jmb.2005.12.082

来源: Elsevier

【 摘 要 】

Caspase-2 is implicated in stress-induced apoptosis that acts as an upstream initiator of mitochondrial permeabilization. Recent studies have shown that caspase-2 activation requires a molecular complex known as the PIDDosome comprising the p53-inducible protein PIDD, the adapter protein RAIDD and caspase-2. RAIDD has an N-terminal caspase recruitment domain (CARD) that interacts with the CARD of caspase-2 and a C-terminal death domain (DD) that interacts with the DD in PIDD. As a first step towards elucidating the molecular mechanisms of caspase-2 activation, we report the crystal structure of RAIDD DD at 2.0 angstrom resolution. The high-resolution structure reveals important features of RAIDD DD that may be important for DD folding and dynamics and for assembly of the PIDDosome. (c) 2005 Elsevier Ltd. All rights reserved.

【 授权许可】

Free