1few

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(New page: 200px<br /> <applet load="1few" size="450" color="white" frame="true" align="right" spinBox="true" caption="1few, resolution 2.2&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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'''CRYSTAL STRUCTURE OF SMAC/DIABLO'''<br />
'''CRYSTAL STRUCTURE OF SMAC/DIABLO'''<br />
==Overview==
==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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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.
==About this Structure==
==About this Structure==
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1FEW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FEW OCA].
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1FEW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FEW OCA].
==Reference==
==Reference==
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[[Category: smac]]
[[Category: smac]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:52:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:54 2008''

Revision as of 10:37, 21 February 2008

Image:1few.gif

1few, resolution 2.2Å

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CRYSTAL STRUCTURE OF SMAC/DIABLO

Overview

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.

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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