1c9q: Difference between revisions

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New page: left|200px<br /> <applet load="1c9q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c9q" /> '''AVERAGE NMR SOLUTION STRUCTURE OF THE BIR-2...
 
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[[Image:1c9q.gif|left|200px]]<br />
[[Image:1c9q.gif|left|200px]]<br /><applet load="1c9q" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1c9q" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1c9q" />
caption="1c9q" />
'''AVERAGE NMR SOLUTION STRUCTURE OF THE BIR-2 DOMAIN OF XIAP'''<br />
'''AVERAGE NMR SOLUTION STRUCTURE OF THE BIR-2 DOMAIN OF XIAP'''<br />


==Overview==
==Overview==
The inhibitor-of-apoptosis (IAP) family of proteins, originally identified, in baculoviruses, regulate programmed cell death in a variety of, organisms. IAPs inhibit specific enzymes (caspases) in the death cascade, and contain one to three modules of a common 70-amino-acid motif called, the BIR domain. Here we describe the nuclear magnetic resonance structure, of a region encompassing the second BIR domain (BIR2) of a human IAP, family member, XIAP (also called hILP or MIHA). The structure of the BIR, domain consists of a three-stranded antiparallel beta-sheet and four, alpha-helices and resembles a classical zinc finger. Unexpectedly, conserved amino acids within the linker region between the BIR1 and BIR2, domains were found to be critical for inhibiting caspase-3. The absence or, presence of these residues may explain the differences in caspase, inhibition observed for different truncated and full-length IAPs. Our data, further indicate that these residues may bind to the active site and that, the BIR domain may interact with an adjacent site on the enzyme.
The inhibitor-of-apoptosis (IAP) family of proteins, originally identified in baculoviruses, regulate programmed cell death in a variety of organisms. IAPs inhibit specific enzymes (caspases) in the death cascade and contain one to three modules of a common 70-amino-acid motif called the BIR domain. Here we describe the nuclear magnetic resonance structure of a region encompassing the second BIR domain (BIR2) of a human IAP family member, XIAP (also called hILP or MIHA). The structure of the BIR domain consists of a three-stranded antiparallel beta-sheet and four alpha-helices and resembles a classical zinc finger. Unexpectedly, conserved amino acids within the linker region between the BIR1 and BIR2 domains were found to be critical for inhibiting caspase-3. The absence or presence of these residues may explain the differences in caspase inhibition observed for different truncated and full-length IAPs. Our data further indicate that these residues may bind to the active site and that the BIR domain may interact with an adjacent site on the enzyme.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1C9Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1C9Q OCA].  
1C9Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1C9Q OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Fesik, S.W.]]
[[Category: Fesik, S W.]]
[[Category: Meadows, R.P.]]
[[Category: Meadows, R P.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: apoptosis]]
[[Category: apoptosis]]
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[[Category: zinc finger]]
[[Category: zinc finger]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:03:53 2008''

Revision as of 13:03, 21 February 2008

File:1c9q.gif


1c9q

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AVERAGE NMR SOLUTION STRUCTURE OF THE BIR-2 DOMAIN OF XIAP

OverviewOverview

The inhibitor-of-apoptosis (IAP) family of proteins, originally identified in baculoviruses, regulate programmed cell death in a variety of organisms. IAPs inhibit specific enzymes (caspases) in the death cascade and contain one to three modules of a common 70-amino-acid motif called the BIR domain. Here we describe the nuclear magnetic resonance structure of a region encompassing the second BIR domain (BIR2) of a human IAP family member, XIAP (also called hILP or MIHA). The structure of the BIR domain consists of a three-stranded antiparallel beta-sheet and four alpha-helices and resembles a classical zinc finger. Unexpectedly, conserved amino acids within the linker region between the BIR1 and BIR2 domains were found to be critical for inhibiting caspase-3. The absence or presence of these residues may explain the differences in caspase inhibition observed for different truncated and full-length IAPs. Our data further indicate that these residues may bind to the active site and that the BIR domain may interact with an adjacent site on the enzyme.

DiseaseDisease

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

About this StructureAbout this Structure

1C9Q is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP., Sun C, Cai M, Gunasekera AH, Meadows RP, Wang H, Chen J, Zhang H, Wu W, Xu N, Ng SC, Fesik SW, Nature. 1999 Oct 21;401(6755):818-22. PMID:10548111

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