1xb0

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[[Image:1xb0.gif|left|200px]]
[[Image:1xb0.gif|left|200px]]
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{{Structure
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|PDB= 1xb0 |SIZE=350|CAPTION= <scene name='initialview01'>1xb0</scene>, resolution 2.2&Aring;
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The line below this paragraph, containing "STRUCTURE_1xb0", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|GENE= BIRC8, ILP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1xb0| PDB=1xb0 | SCENE= }}
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|RELATEDENTRY=[[1xb1|1XB1]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xb0 OCA], [http://www.ebi.ac.uk/pdbsum/1xb0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xb0 RCSB]</span>
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'''Structure of the BIR domain of IAP-like protein 2'''
'''Structure of the BIR domain of IAP-like protein 2'''
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[[Category: Sampaio, C A.M.]]
[[Category: Sampaio, C A.M.]]
[[Category: Shin, H.]]
[[Category: Shin, H.]]
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[[Category: apoptosis]]
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[[Category: Apoptosis]]
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[[Category: caspase inhibition]]
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[[Category: Caspase inhibition]]
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[[Category: diablo]]
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[[Category: Diablo]]
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[[Category: smac]]
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[[Category: Smac]]
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[[Category: xiap]]
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[[Category: Xiap]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:48:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:47:08 2008''
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Revision as of 11:48, 3 May 2008

Template:STRUCTURE 1xb0

Structure of the BIR domain of IAP-like protein 2


Overview

Several IAP (inhibitor of apoptosis) proteins regulate cell fate decisions, and the X-linked IAP (XIAP) does so in part by inhibiting caspases, proteases that execute the apoptotic pathway. A tissue-specific homologue of XIAP, known as ILP2 (IAP-like protein 2), has previously been implicated in the control of apoptosis in the testis by direct inhibition of caspase 9. In examining this protein we found that the putative caspase 9 interaction domain is a surprisingly weak inhibitor and is also conformationally unstable. Comparison with the equivalent domain in XIAP demonstrated that the instability is due to the lack of a linker segment N-terminal to the inhibitory BIR (baculovirus IAP repeat) domain. Fusion of a 9-residue linker from XIAP to the N-terminus of ILP2 restored tight caspase 9 inhibition, dramatically increased conformational stability and allowed crystallization of the ILP2 BIR domain in a form strikingly similar to the XIAP third BIR domain. We conclude that ILP2 is an unstable protein, and cannot inhibit caspase 9 in a physiological way on its own. We speculate that ILP2 requires assistance from unidentified cellular factors to be an effective inhibitor of apoptosis in vivo.

About this Structure

1XB0 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The BIR domain of IAP-like protein 2 is conformationally unstable: implications for caspase inhibition., Shin H, Renatus M, Eckelman BP, Nunes VA, Sampaio CA, Salvesen GS, Biochem J. 2005 Jan 1;385(Pt 1):1-10. PMID:15485395 Page seeded by OCA on Sat May 3 14:48:02 2008

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