1few: Difference between revisions

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{{STRUCTURE_1few|  PDB=1few  |  SCENE=  }}  
{{STRUCTURE_1few|  PDB=1few  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF SMAC/DIABLO'''
===CRYSTAL STRUCTURE OF SMAC/DIABLO===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_10972280}}, adds the Publication Abstract to the page
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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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