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http://purl.uniprot.org/citations/11967569http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11967569http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11967569http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/11967569http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.org/dc/terms/identifier"doi:10.1038/nsb795"xsd:string
http://purl.uniprot.org/citations/11967569http://purl.org/dc/terms/identifier"doi:10.1038/nsb795"xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Li P."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Li P."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Li W."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Li W."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Shi Y."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Shi Y."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Zhang Z."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Zhang Z."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Alnemri E.S."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Alnemri E.S."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Wu J.W."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Wu J.W."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Chai J."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Chai J."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Srinivasula S.M."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/author"Srinivasula S.M."xsd:string
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11967569http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string