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1i4o

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(New page: 200px<br /> <applet load="1i4o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i4o, resolution 2.4&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1i4o.gif|left|200px]]<br />
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[[Image:1i4o.gif|left|200px]]<br /><applet load="1i4o" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1i4o" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1i4o, resolution 2.4&Aring;" />
caption="1i4o, resolution 2.4&Aring;" />
'''CRYSTAL STRUCTURE OF THE XIAP/CASPASE-7 COMPLEX'''<br />
'''CRYSTAL STRUCTURE OF THE XIAP/CASPASE-7 COMPLEX'''<br />
==Overview==
==Overview==
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The inhibitor of apoptosis proteins (IAPs) represent the only endogenous, caspase inhibitors and are characterized by the presence of baculoviral, IAP repeats (BIRs). Here, we report the crystal structure of the complex, between human caspase-7 and XIAP (BIR2 and the proceeding linker). The, structure surprisingly reveals that the linker is the only contacting, element for the caspase, while the BIR2 domain is invisible in the, crystal. The linker interacts with and blocks the substrate groove of the, caspase in a backward fashion, distinct from substrate recognition., Structural analyses suggest that the linker is the energetic and, specificity determinant of the interaction. Further biochemical, characterizations clearly establish that the linker harbors the major, energetic determinant, while the BIR2 domain serves as a regulatory, element for caspase binding and Smac neutralization.
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The inhibitor of apoptosis proteins (IAPs) represent the only endogenous caspase inhibitors and are characterized by the presence of baculoviral IAP repeats (BIRs). Here, we report the crystal structure of the complex between human caspase-7 and XIAP (BIR2 and the proceeding linker). The structure surprisingly reveals that the linker is the only contacting element for the caspase, while the BIR2 domain is invisible in the crystal. The linker interacts with and blocks the substrate groove of the caspase in a backward fashion, distinct from substrate recognition. Structural analyses suggest that the linker is the energetic and specificity determinant of the interaction. Further biochemical characterizations clearly establish that the linker harbors the major energetic determinant, while the BIR2 domain serves as a regulatory element for caspase binding and Smac neutralization.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1I4O 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=1I4O OCA].
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1I4O 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=1I4O OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Huang, Y.]]
[[Category: Huang, Y.]]
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[[Category: Myszka, D.G.]]
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[[Category: Myszka, D G.]]
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[[Category: Park, Y.C.]]
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[[Category: Park, Y C.]]
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[[Category: Rich, R.L.]]
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[[Category: Rich, R L.]]
[[Category: Segal, D.]]
[[Category: Segal, D.]]
[[Category: Wu, H.]]
[[Category: Wu, H.]]
[[Category: protease-inhibitor]]
[[Category: protease-inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:26:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:57 2008''

Revision as of 11:07, 21 February 2008


1i4o, resolution 2.4Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE XIAP/CASPASE-7 COMPLEX

Contents

Overview

The inhibitor of apoptosis proteins (IAPs) represent the only endogenous caspase inhibitors and are characterized by the presence of baculoviral IAP repeats (BIRs). Here, we report the crystal structure of the complex between human caspase-7 and XIAP (BIR2 and the proceeding linker). The structure surprisingly reveals that the linker is the only contacting element for the caspase, while the BIR2 domain is invisible in the crystal. The linker interacts with and blocks the substrate groove of the caspase in a backward fashion, distinct from substrate recognition. Structural analyses suggest that the linker is the energetic and specificity determinant of the interaction. Further biochemical characterizations clearly establish that the linker harbors the major energetic determinant, while the BIR2 domain serves as a regulatory element for caspase binding and Smac neutralization.

Disease

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

About this Structure

1I4O is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain., Huang Y, Park YC, Rich RL, Segal D, Myszka DG, Wu H, Cell. 2001 Mar 9;104(5):781-90. PMID:11257231

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