1i3o

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(New page: 200px<br /> <applet load="1i3o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i3o, resolution 2.7&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1i3o.gif|left|200px]]<br />
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[[Image:1i3o.gif|left|200px]]<br /><applet load="1i3o" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1i3o" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1i3o, resolution 2.7&Aring;" />
caption="1i3o, resolution 2.7&Aring;" />
'''CRYSTAL STRUCTURE OF THE COMPLEX OF XIAP-BIR2 AND CASPASE 3'''<br />
'''CRYSTAL STRUCTURE OF THE COMPLEX OF XIAP-BIR2 AND CASPASE 3'''<br />
==Overview==
==Overview==
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The molecular mechanism(s) that regulate apoptosis by caspase inhibition, remain poorly understood. The main endogenous inhibitors are members of, the IAP family and are exemplified by XIAP, which regulates the initiator, caspase-9, and the executioner caspases-3 and -7. We report the crystal, structure of the second BIR domain of XIAP (BIR2) in complex with, caspase-3, at a resolution of 2.7 A, revealing the structural basis for, inhibition. The inhibitor makes limited contacts through its BIR domain to, the surface of the enzyme, and most contacts to caspase-3 originate from, the N-terminal extension. This lies across the substrate binding cleft, but in reverse orientation compared to substrate binding. The mechanism of, inhibition is due to a steric blockade prohibitive of substrate binding, and is distinct from the mechanism utilized by synthetic substrate analog, inhibitors.
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The molecular mechanism(s) that regulate apoptosis by caspase inhibition remain poorly understood. The main endogenous inhibitors are members of the IAP family and are exemplified by XIAP, which regulates the initiator caspase-9, and the executioner caspases-3 and -7. We report the crystal structure of the second BIR domain of XIAP (BIR2) in complex with caspase-3, at a resolution of 2.7 A, revealing the structural basis for inhibition. The inhibitor makes limited contacts through its BIR domain to the surface of the enzyme, and most contacts to caspase-3 originate from the N-terminal extension. This lies across the substrate binding cleft, but in reverse orientation compared to substrate binding. The mechanism of inhibition is due to a steric blockade prohibitive of substrate binding, and is distinct from the mechanism utilized by synthetic substrate analog inhibitors.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1I3O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I3O OCA].
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1I3O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I3O OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Fesik, S.W.]]
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[[Category: Fesik, S W.]]
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[[Category: Liddington, R.C.]]
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[[Category: Liddington, R C.]]
[[Category: Renatus, M.]]
[[Category: Renatus, M.]]
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[[Category: Riedl, S.J.]]
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[[Category: Riedl, S J.]]
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[[Category: Salvesen, G.S.]]
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[[Category: Salvesen, G S.]]
[[Category: Schwarzenbacher, R.]]
[[Category: Schwarzenbacher, R.]]
[[Category: Sun, C.]]
[[Category: Sun, C.]]
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[[Category: iap]]
[[Category: iap]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:25:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:42 2008''

Revision as of 11:07, 21 February 2008

Image:1i3o.gif

1i3o, resolution 2.7Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE COMPLEX OF XIAP-BIR2 AND CASPASE 3

Contents

Overview

The molecular mechanism(s) that regulate apoptosis by caspase inhibition remain poorly understood. The main endogenous inhibitors are members of the IAP family and are exemplified by XIAP, which regulates the initiator caspase-9, and the executioner caspases-3 and -7. We report the crystal structure of the second BIR domain of XIAP (BIR2) in complex with caspase-3, at a resolution of 2.7 A, revealing the structural basis for inhibition. The inhibitor makes limited contacts through its BIR domain to the surface of the enzyme, and most contacts to caspase-3 originate from the N-terminal extension. This lies across the substrate binding cleft, but in reverse orientation compared to substrate binding. The mechanism of inhibition is due to a steric blockade prohibitive of substrate binding, and is distinct from the mechanism utilized by synthetic substrate analog inhibitors.

Disease

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

About this Structure

1I3O is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structural basis for the inhibition of caspase-3 by XIAP., Riedl SJ, Renatus M, Schwarzenbacher R, Zhou Q, Sun C, Fesik SW, Liddington RC, Salvesen GS, Cell. 2001 Mar 9;104(5):791-800. PMID:11257232

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