2of5 | pdb_00002of5
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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
Page seeded by OCA on Mon Nov 12 23:10:19 2007
