1f9x
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(New page: 200px<br /> <applet load="1f9x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f9x" /> '''AVERAGE NMR SOLUTION STRUCTURE OF THE BIR-3...)
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Revision as of 14:44, 12 November 2007
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AVERAGE NMR SOLUTION STRUCTURE OF THE BIR-3 DOMAIN OF XIAP
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Lymphoproliferative syndrome, X-linked, 2 OMIM:[300079]
About this Structure
1F9X is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
Reference
NMR structure and mutagenesis of the third Bir domain of the inhibitor of apoptosis protein XIAP., Sun C, Cai M, Meadows RP, Xu N, Gunasekera AH, Herrmann J, Wu JC, Fesik SW, J Biol Chem. 2000 Oct 27;275(43):33777-81. PMID:10934209
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