Crystal Structure of RAIDD Death Domain Implicates Potential Mechanism of PIDDosome Assembly

Journal Article · Sun Jan 01 04:00:00 EST 2006 · J. Mol. Biol.

DOI:https://doi.org/10.1016/j.jmb.2005.12.082· OSTI ID:914023

Park, H; Wu, H

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 Angstroms 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.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 914023
• Report Number(s): BNL--78591-2007-JA
• Journal Information: J. Mol. Biol., Journal Name: J. Mol. Biol. Journal Issue: 2 Vol. 357; ISSN JMOBAK; ISSN 0022-2836
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
43 PARTICLE ACCELERATORS
APOPTOSIS
CRYSTAL STRUCTURE
DEATH
NSLS
PROTEINS
RESOLUTION
national synchrotron light source