1i4o
From Proteopedia
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| - | [[Image:1i4o.gif|left|200px]] | + | [[Image:1i4o.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE XIAP/CASPASE-7 COMPLEX''' | + | {{Structure |
| + | |PDB= 1i4o |SIZE=350|CAPTION= <scene name='initialview01'>1i4o</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF THE XIAP/CASPASE-7 COMPLEX''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1I4O is a [ | + | 1I4O is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11257231 11257231] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: protease-inhibitor]] | [[Category: protease-inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:45:31 2008'' |
Revision as of 09:45, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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