NDLI: NMR structure and mutagenesis of the third Bir domain of the inhibitor of apoptosis protein XIAP.

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NMR structure and mutagenesis of the third Bir domain of the inhibitor of apoptosis protein XIAP.

Content Provider	Semantic Scholar
Author	Sun, Chaohong C. Cai, Mingmei Xu, Ning Herrmann, João Lourenço
Copyright Year	2000
Abstract	The inhibitor of apoptosis proteins (IAPs) regulate the caspase family of cysteine proteases, which play an important role in the execution of programmed cell death. Human X-linked inhibitor of apoptosis protein (XIAP) is a potent inhibitor of caspases-3, -7, and -9. Here we show that the Bir3 domain is the minimal region of XIAP that is needed for potent caspase-9 inhibition. The three-dimensional structure of the Bir3 domain of XIAP, determined by NMR spectroscopy, resembles a classical zinc finger and consists of five alpha-helices, a three-stranded beta-sheet, and a zinc atom chelated to three cysteines and one histidine. The structure of the Bir3 domain is similar to that of the Bir2 domain of XIAP but differs from the previously determined structure of the Bir3 domain of MIHB. Based on site-directed mutagenesis, we have identified the regions of the Bir3 domain of XIAP that are important for inhibiting caspase-9. Despite the structural similarities of the Bir2 and Bir3 domain of XIAP, a different set of residues were found to be critical for inhibiting the individual caspases. These results suggest that XIAP inhibits caspase-3 and caspase-9 in a different manner.
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.jbc.org/content/early/2000/08/08/jbc.M006226200.full.pdf
PubMed reference number	10934209v1
Volume Number	275
Issue Number	43
Journal	The Journal of biological chemistry
Language	English
Access Restriction	Open
Subject Keyword	Apoptosis BIRC2 gene Cell Death Cysteine Histidine Inhibition Intracisternal A-Particle Elements Mutagenesis, Site-Directed X-Ray Emission Spectroscopy XIAP gene Zinc Fingers caspase caspase-3 caspase-9 inhibitor-of-apoptosis protein
Content Type	Text
Resource Type	Article

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