2OF5

Oligomeric Death Domain complex

2OF5 の概要

• エントリーDOI: 10.2210/pdb2of5/pdb
• 分子名称: Death domain-containing protein CRADD, Leucine-rich repeat and death domain-containing protein (3 entities in total)
• 機能のキーワード: death domain complex, apoptosis
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm (By similarity): P78560; Cytoplasm: Q9HB75
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 158675.35

構造登録者

Park, H.H.,Logette, E.,Raunser, S.,Cuenin, S.,Walz, T.,Tschopp, J.,Wu, H. (登録日: 2007-01-02, 公開日: 2007-04-17, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.2 Å)