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1i51

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(New page: 200px<br /> <applet load="1i51" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i51, resolution 2.45&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1i51.gif|left|200px]]<br /><applet load="1i51" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1i51" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1i51, resolution 2.45&Aring;" />
caption="1i51, resolution 2.45&Aring;" />
'''CRYSTAL STRUCTURE OF CASPASE-7 COMPLEXED WITH XIAP'''<br />
'''CRYSTAL STRUCTURE OF CASPASE-7 COMPLEXED WITH XIAP'''<br />
==Overview==
==Overview==
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The inhibitor of apoptosis (IAP) proteins suppress cell death by, inhibiting the catalytic activity of caspases. Here we present the crystal, structure of caspase-7 in complex with a potent inhibitory fragment from, XIAP at 2.45 A resolution. An 18-residue XIAP peptide binds the catalytic, groove of caspase-7, making extensive contacts to the residues that are, essential for its catalytic activity. Strikingly, despite a reversal of, relative orientation, a subset of interactions between caspase-7 and XIAP, closely resemble those between caspase-7 and its tetrapeptide inhibitor, DEVD-CHO. Our biochemical and structural analyses reveal that the BIR, domains are dispensable for the inhibition of caspase-3 and -7. This study, provides a structural basis for the design of the next-generation caspase, inhibitors.
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The inhibitor of apoptosis (IAP) proteins suppress cell death by inhibiting the catalytic activity of caspases. Here we present the crystal structure of caspase-7 in complex with a potent inhibitory fragment from XIAP at 2.45 A resolution. An 18-residue XIAP peptide binds the catalytic groove of caspase-7, making extensive contacts to the residues that are essential for its catalytic activity. Strikingly, despite a reversal of relative orientation, a subset of interactions between caspase-7 and XIAP closely resemble those between caspase-7 and its tetrapeptide inhibitor DEVD-CHO. Our biochemical and structural analyses reveal that the BIR domains are dispensable for the inhibition of caspase-3 and -7. This study provides a structural basis for the design of the next-generation caspase inhibitors.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1I51 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1I51 OCA].
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1I51 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1I51 OCA].
==Reference==
==Reference==
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[[Category: protease]]
[[Category: protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:26:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:06 2008''

Revision as of 11:08, 21 February 2008

Image:1i51.gif

1i51, resolution 2.45Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF CASPASE-7 COMPLEXED WITH XIAP

Contents

Overview

The inhibitor of apoptosis (IAP) proteins suppress cell death by inhibiting the catalytic activity of caspases. Here we present the crystal structure of caspase-7 in complex with a potent inhibitory fragment from XIAP at 2.45 A resolution. An 18-residue XIAP peptide binds the catalytic groove of caspase-7, making extensive contacts to the residues that are essential for its catalytic activity. Strikingly, despite a reversal of relative orientation, a subset of interactions between caspase-7 and XIAP closely resemble those between caspase-7 and its tetrapeptide inhibitor DEVD-CHO. Our biochemical and structural analyses reveal that the BIR domains are dispensable for the inhibition of caspase-3 and -7. This study provides a structural basis for the design of the next-generation caspase inhibitors.

Disease

Known diseases associated with this structure: Lymphoproliferative syndrome, X-linked, 2 OMIM:[300079]

About this Structure

1I51 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of caspase-7 inhibition by XIAP., Chai J, Shiozaki E, Srinivasula SM, Wu Q, Datta P, Alnemri ES, Shi Y, Cell. 2001 Mar 9;104(5):769-80. PMID:11257230

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