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

Abstract

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.

Authors:
;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
914023
Report Number(s):
BNL-78591-2007-JA
Journal ID: ISSN 0022-2836; JMOBAK; TRN: US0801481
DOE Contract Number:
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: J. Mol. Biol.; Journal Volume: 357; Journal Issue: 2
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; 43 PARTICLE ACCELERATORS; APOPTOSIS; CRYSTAL STRUCTURE; DEATH; PROTEINS; RESOLUTION; NSLS; national synchrotron light source

Citation Formats

Park,H., and Wu, H.. Crystal Structure of RAIDD Death Domain Implicates Potential Mechanism of PIDDosome Assembly. United States: N. p., 2006. Web. doi:10.1016/j.jmb.2005.12.082.
Park,H., & Wu, H.. Crystal Structure of RAIDD Death Domain Implicates Potential Mechanism of PIDDosome Assembly. United States. doi:10.1016/j.jmb.2005.12.082.
Park,H., and Wu, H.. Sun . "Crystal Structure of RAIDD Death Domain Implicates Potential Mechanism of PIDDosome Assembly". United States. doi:10.1016/j.jmb.2005.12.082.
@article{osti_914023,
title = {Crystal Structure of RAIDD Death Domain Implicates Potential Mechanism of PIDDosome Assembly},
author = {Park,H. and Wu, H.},
abstractNote = {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.},
doi = {10.1016/j.jmb.2005.12.082},
journal = {J. Mol. Biol.},
number = 2,
volume = 357,
place = {United States},
year = {Sun Jan 01 00:00:00 EST 2006},
month = {Sun Jan 01 00:00:00 EST 2006}
}