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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2006-3-1
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pubmed:abstractText |
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 A 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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-10347191,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-10376594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-10589682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-10964568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-10973264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-11983156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-12040174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-12193789,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-12463158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-12655293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-14573612,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-14646132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-14744432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-15073321,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-15226512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-15299354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-15520809,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-15654015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-15656350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-15865942,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-1758883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-2184035,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-7538907,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-7684370,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-8087842,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-8347566,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-8397073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-8521815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-8612133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-8681376,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-8681377,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16434054-9828010
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/CRADD Signaling Adaptor Protein,
http://linkedlifedata.com/resource/pubmed/chemical/CRADD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Death Domain Receptor Signaling...,
http://linkedlifedata.com/resource/pubmed/chemical/FADD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fas-Associated Death Domain Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/PIDD protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
357
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
358-64
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:16434054-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:16434054-Amino Acid Sequence,
pubmed-meshheading:16434054-Animals,
pubmed-meshheading:16434054-Apoptosis,
pubmed-meshheading:16434054-CRADD Signaling Adaptor Protein,
pubmed-meshheading:16434054-Carrier Proteins,
pubmed-meshheading:16434054-Caspase 2,
pubmed-meshheading:16434054-Caspases,
pubmed-meshheading:16434054-Crystallography, X-Ray,
pubmed-meshheading:16434054-Death Domain Receptor Signaling Adaptor Proteins,
pubmed-meshheading:16434054-Enzyme Activation,
pubmed-meshheading:16434054-Fas-Associated Death Domain Protein,
pubmed-meshheading:16434054-Humans,
pubmed-meshheading:16434054-Models, Molecular,
pubmed-meshheading:16434054-Molecular Sequence Data,
pubmed-meshheading:16434054-Multiprotein Complexes,
pubmed-meshheading:16434054-Protein Conformation,
pubmed-meshheading:16434054-Sequence Alignment,
pubmed-meshheading:16434054-Sequence Homology, Amino Acid
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pubmed:year |
2006
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pubmed:articleTitle |
Crystal structure of RAIDD death domain implicates potential mechanism of PIDDosome assembly.
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pubmed:affiliation |
Department of Biochemistry, Weill Medical College and Graduate School of Medical Sciences of Cornell University, New York, NY 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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