2of5
From Proteopedia
(New page: 200px<br /> <applet load="2of5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2of5, resolution 3.2Å" /> '''Oligomeric Death Dom...) |
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| - | [[Image:2of5.gif|left|200px]]<br /> | + | [[Image:2of5.gif|left|200px]]<br /><applet load="2of5" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2of5" size=" | + | |
caption="2of5, resolution 3.2Å" /> | caption="2of5, resolution 3.2Å" /> | ||
'''Oligomeric Death Domain complex'''<br /> | '''Oligomeric Death Domain complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Proteins of the death domain (DD) superfamily mediate assembly of | + | Proteins of the death domain (DD) superfamily mediate assembly of oligomeric signaling complexes for the activation of caspases and kinases via unknown mechanisms. Here we report the crystal structure of the PIDD DD and RAIDD DD complex, which forms the core of the caspase-2-activating complex PIDDosome. Although RAIDD DD and PIDD DD are monomers, they assemble into a complex that comprises seven RAIDD DDs and five PIDD DDs. Despite the use of an asymmetric assembly mechanism, all DDs in the complex are in quasi-equivalent environments. The structure provided eight unique asymmetric interfaces, which can be classified into three types. These three types of interactions together cover a majority of the DD surface. Mutagenesis on almost all interfaces leads to disruption of the assembly, resulting in defective caspase-2 activation. The three types of interactions may represent most, if not all, modes of interactions in the DD superfamily for assembling complexes of different stoichiometry. |
==About this Structure== | ==About this Structure== | ||
| - | 2OF5 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:// | + | 2OF5 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=2OF5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cuenin, S.]] | [[Category: Cuenin, S.]] | ||
[[Category: Logette, E.]] | [[Category: Logette, E.]] | ||
| - | [[Category: Park, H | + | [[Category: Park, H H.]] |
[[Category: Raunser, S.]] | [[Category: Raunser, S.]] | ||
[[Category: Tschopp, J.]] | [[Category: Tschopp, J.]] | ||
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[[Category: death domain complex]] | [[Category: death domain complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:17:47 2008'' |
Revision as of 16:17, 21 February 2008
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Oligomeric Death Domain complex
Overview
Proteins of the death domain (DD) superfamily mediate assembly of oligomeric signaling complexes for the activation of caspases and kinases via unknown mechanisms. Here we report the crystal structure of the PIDD DD and RAIDD DD complex, which forms the core of the caspase-2-activating complex PIDDosome. Although RAIDD DD and PIDD DD are monomers, they assemble into a complex that comprises seven RAIDD DDs and five PIDD DDs. Despite the use of an asymmetric assembly mechanism, all DDs in the complex are in quasi-equivalent environments. The structure provided eight unique asymmetric interfaces, which can be classified into three types. These three types of interactions together cover a majority of the DD surface. Mutagenesis on almost all interfaces leads to disruption of the assembly, resulting in defective caspase-2 activation. The three types of interactions may represent most, if not all, modes of interactions in the DD superfamily for assembling complexes of different stoichiometry.
About this Structure
2OF5 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex., Park HH, Logette E, Raunser S, Cuenin S, Walz T, Tschopp J, Wu H, Cell. 2007 Feb 9;128(3):533-46. PMID:17289572
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