1F3V

Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2

1F3V の概要

• エントリーDOI: 10.2210/pdb1f3v/pdb
• 分子名称: TUMOR NECROSIS FACTOR RECEPTOR TYPE 1 ASSOCIATED DEATH DOMAIN PROTEIN, TUMOR NECROSIS FACTOR RECEPTOR-ASSOCIATED PROTEIN (3 entities in total)
• 機能のキーワード: a-b sandwich, apoptosis
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus : Q15628; Cytoplasm : Q12933
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39131.64

構造登録者

Park, Y.C.,Ye, H.,Hsia, C.,Segal, D.,Rich, R.,Liou, H.-C.,Myszka, D.,Wu, H. (登録日: 2000-06-06, 公開日: 2000-09-06, 最終更新日: 2024-11-13)

主引用文献

Park, Y.C.,Ye, H.,Hsia, C.,Segal, D.,Rich, R.L.,Liou, H.C.,Myszka, D.G.,Wu, H.
A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction.
Cell(Cambridge,Mass.), 101:777-787, 2000

PubMed Abstract: TRAF proteins are major mediators for the cell activation, cell survival, and antiapoptotic functions of the TNF receptor superfamily. They can be recruited to activated TNF receptors either by direct interactions with the receptors or indirectly via the adaptor protein TRADD. We now report the structure of the TRADD-TRAF2 complex, which is highly distinct from receptor-TRAF2 interactions. This interaction is significantly stronger and we show by an in vivo signaling assay that TRAF2 signaling is more readily initiated by TRADD than by direct receptor-TRAF2 interactions. TRADD is specific for TRAF1 and TRAF2, which ensures the recruitment of clAPs for the direct inhibition of caspase activation in the signaling complex. The stronger affinity and unique specificity of the TRADD-TRAF2 interaction are crucial for the suppression of apoptosis and provide a mechanistic basis for the perturbation of TRAF recruitment in sensitizing cell death induction.

PubMed: 10892748
DOI: 10.1016/S0092-8674(00)80889-2

実験手法

X-RAY DIFFRACTION (2 Å)