1few

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[[Image:1few.png|left|200px]]
 
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{{STRUCTURE_1few| PDB=1few | SCENE= }}
{{STRUCTURE_1few| PDB=1few | SCENE= }}
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===CRYSTAL STRUCTURE OF SMAC/DIABLO===
===CRYSTAL STRUCTURE OF SMAC/DIABLO===
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{{ABSTRACT_PUBMED_10972280}}
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{{ABSTRACT_PUBMED_10972280}}
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==Disease==
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[[http://www.uniprot.org/uniprot/DBLOH_HUMAN DBLOH_HUMAN]] Defects in DIABLO are the cause of deafness autosomal dominant type 64 (DFNA64) [MIM:[http://omim.org/entry/614152 614152]]. DFNA64 is a form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.<ref>PMID:21722859</ref>
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==Function==
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[[http://www.uniprot.org/uniprot/DBLOH_HUMAN DBLOH_HUMAN]] Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases. Isoform 3 attenuates the stability and apoptosis-inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-proteasome pathway. Isoform 3 also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. Isoform 1 is defective in the capacity to down-regulate the XIAP/BIRC4 abundance.<ref>PMID:10929711</ref><ref>PMID:14523016</ref><ref>PMID:15200957</ref>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:010972280</ref><references group="xtra"/>
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<ref group="xtra">PMID:010972280</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Chai, J.]]
[[Category: Chai, J.]]

Revision as of 00:31, 25 March 2013

Template:STRUCTURE 1few

Contents

CRYSTAL STRUCTURE OF SMAC/DIABLO

Template:ABSTRACT PUBMED 10972280

Disease

[DBLOH_HUMAN] Defects in DIABLO are the cause of deafness autosomal dominant type 64 (DFNA64) [MIM:614152]. DFNA64 is a form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.[1]

Function

[DBLOH_HUMAN] Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases. Isoform 3 attenuates the stability and apoptosis-inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-proteasome pathway. Isoform 3 also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. Isoform 1 is defective in the capacity to down-regulate the XIAP/BIRC4 abundance.[2][3][4]

About this Structure

1few is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  1. ↑ Cheng J, Zhu Y, He S, Lu Y, Chen J, Han B, Petrillo M, Wrzeszczynski KO, Yang S, Dai P, Zhai S, Han D, Zhang MQ, Li W, Liu X, Li H, Chen ZY, Yuan H. Functional mutation of SMAC/DIABLO, encoding a mitochondrial proapoptotic protein, causes human progressive hearing loss DFNA64. Am J Hum Genet. 2011 Jul 15;89(1):56-66. doi: 10.1016/j.ajhg.2011.05.027. Epub, 2011 Jun 30. PMID:21722859 doi:10.1016/j.ajhg.2011.05.027
  2. ↑ Du C, Fang M, Li Y, Li L, Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell. 2000 Jul 7;102(1):33-42. PMID:10929711
  3. ↑ Fu J, Jin Y, Arend LJ. Smac3, a novel Smac/DIABLO splicing variant, attenuates the stability and apoptosis-inhibiting activity of X-linked inhibitor of apoptosis protein. J Biol Chem. 2003 Dec 26;278(52):52660-72. Epub 2003 Sep 30. PMID:14523016 doi:10.1074/jbc.M308036200
  4. ↑ Bartke T, Pohl C, Pyrowolakis G, Jentsch S. Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase. Mol Cell. 2004 Jun 18;14(6):801-11. PMID:15200957 doi:10.1016/j.molcel.2004.05.018

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