Source:http://linkedlifedata.com/resource/pubmed/id/11967569
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
2002-5-28
|
| pubmed:databankReference | |
| pubmed:abstractText |
HtrA2/Omi, a mitochondrial serine protease in mammals, is important in programmed cell death. However, the underlining mechanism of HtrA2/Omi-mediated apoptosis remains unclear. Analogous to the bacterial homolog HtrA (DegP), the mature HtrA2 protein contains a central serine protease domain and a C-terminal PDZ domain. The 2.0 A crystal structure of HtrA2/Omi reveals the formation of a pyramid-shaped homotrimer mediated exclusively by the serine protease domains. The peptide-binding pocket of the PDZ domain is buried in the intimate interface between the PDZ and the protease domains. Mutational analysis reveals that the monomeric HtrA2/Omi mutants are unable to induce cell death and are deficient in protease activity. The PDZ domain modulates HtrA2/Omi-mediated cell death activity by regulating its serine protease activity. These structural and biochemical observations provide an important framework for deciphering the mechanisms of HtrA2/Omi-mediated apoptosis.
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| pubmed:commentsCorrections | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
1072-8368
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
9
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
436-41
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11967569-Amino Acid Sequence,
pubmed-meshheading:11967569-Apoptosis,
pubmed-meshheading:11967569-Caspases,
pubmed-meshheading:11967569-Cell Line,
pubmed-meshheading:11967569-Crystallography, X-Ray,
pubmed-meshheading:11967569-Enzyme Activation,
pubmed-meshheading:11967569-Humans,
pubmed-meshheading:11967569-Mitochondria,
pubmed-meshheading:11967569-Mitochondrial Proteins,
pubmed-meshheading:11967569-Models, Molecular,
pubmed-meshheading:11967569-Molecular Sequence Data,
pubmed-meshheading:11967569-Protein Structure, Quaternary,
pubmed-meshheading:11967569-Protein Structure, Secondary,
pubmed-meshheading:11967569-Protein Structure, Tertiary,
pubmed-meshheading:11967569-Sequence Alignment,
pubmed-meshheading:11967569-Serine Endopeptidases,
pubmed-meshheading:11967569-Structure-Activity Relationship
|
| pubmed:year |
2002
|
| pubmed:articleTitle |
Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi.
|
| pubmed:affiliation |
Department of Molecular Biology, Lewis Thomas Laboratory, Princeton University, Princeton, New Jersey 08544, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|