2OF5

Oligomeric Death Domain complex

Summary for 2OF5

• Entry DOI: 10.2210/pdb2of5/pdb
• Descriptor: Death domain-containing protein CRADD, Leucine-rich repeat and death domain-containing protein (3 entities in total)
• Functional Keywords: death domain complex, apoptosis
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm (By similarity): P78560; Cytoplasm: Q9HB75
• Total number of polymer chains: 12
• Total formula weight: 158675.35

Authors

Park, H.H.,Logette, E.,Raunser, S.,Cuenin, S.,Walz, T.,Tschopp, J.,Wu, H. (deposition date: 2007-01-02, release date: 2007-04-17, Last modification date: 2023-12-27)

Primary citation

Park, H.H.,Logette, E.,Raunser, S.,Cuenin, S.,Walz, T.,Tschopp, J.,Wu, H.
Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex.
Cell(Cambridge,Mass.), 128:533-546, 2007

PubMed Abstract: 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.

PubMed: 17289572
DOI: 10.1016/j.cell.2007.01.019

Experimental method

X-RAY DIFFRACTION (3.2 Å)