Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-06-01

AUTHORS

Wenyu Li, Srinivasa M Srinivasula, Jijie Chai, Pingwei Li, Jia-Wei Wu, ZhiJia Zhang, Emad S Alnemri, Yigong Shi

ABSTRACT

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. More... »

PAGES

436-441

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsb795

DOI

http://dx.doi.org/10.1038/nsb795

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1046644737

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11967569


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