1few

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{{STRUCTURE_1few| PDB=1few | SCENE= }}
{{STRUCTURE_1few| PDB=1few | SCENE= }}
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'''CRYSTAL STRUCTURE OF SMAC/DIABLO'''
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===CRYSTAL STRUCTURE OF SMAC/DIABLO===
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==Overview==
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Apoptosis (programmed cell death), an essential process in the development and homeostasis of metazoans, is carried out by caspases. The mitochondrial protein Smac/DIABLO performs a critical function in apoptosis by eliminating the inhibitory effect of IAPs (inhibitor of apoptosis proteins) on caspases. Here we show that Smac/DIABLO promotes not only the proteolytic activation of procaspase-3 but also the enzymatic activity of mature caspase-3, both of which depend upon its ability to interact physically with IAPs. The crystal structure of Smac/DIABLO at 2.2 A resolution reveals that it homodimerizes through an extensive hydrophobic interface. Missense mutations inactivating this dimeric interface significantly compromise the function of Smac/DIABLO. As in the Drosophila proteins Reaper, Grim and Hid, the amino-terminal amino acids of Smac/DIABLO are indispensable for its function, and a seven-residue peptide derived from the amino terminus promotes procaspase-3 activation in vitro. These results establish an evolutionarily conserved structural and biochemical basis for the activation of apoptosis by Smac/DIABLO.
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{{ABSTRACT_PUBMED_10972280}}
==About this Structure==
==About this Structure==
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[[Category: Iap inhibition]]
[[Category: Iap inhibition]]
[[Category: Smac]]
[[Category: Smac]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:14:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:08:36 2008''

Revision as of 00:08, 1 July 2008

Template:STRUCTURE 1few

CRYSTAL STRUCTURE OF SMAC/DIABLO

Template:ABSTRACT PUBMED 10972280

About this Structure

1FEW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural and biochemical basis of apoptotic activation by Smac/DIABLO., Chai J, Du C, Wu JW, Kyin S, Wang X, Shi Y, Nature. 2000 Aug 24;406(6798):855-62. PMID:10972280

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