1D0J

STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A M4-1BB PEPTIDE

1D0J の概要

• エントリーDOI: 10.2210/pdb1d0j/pdb
• 関連するPDBエントリー: 1CA4 1CA9 1CZY 1CZZ 1D00 1D01
• 分子名称: TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED PROTEIN 2, 4-1BB LIGAND RECEPTOR (3 entities in total)
• 機能のキーワード: b-sandwich, protein-peptide complex, apoptosis
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm : Q12933; Membrane; Single-pass type I membrane protein: P20334
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 117189.58

構造登録者

Ye, H.,Park, Y.C.,Kreishman, M.,Kieff, E.,Wu, H. (登録日: 1999-09-10, 公開日: 2000-03-08, 最終更新日: 2024-11-06)

主引用文献

Ye, H.,Park, Y.C.,Kreishman, M.,Kieff, E.,Wu, H.
The structural basis for the recognition of diverse receptor sequences by TRAF2.
Mol.Cell, 4:321-330, 1999

PubMed Abstract: Many members of the tumor necrosis factor receptor (TNFR) superfamily initiate intracellular signaling by recruiting TNFR-associated factors (TRAFs) through their cytoplasmic tails. TRAFs apparently recognize highly diverse receptor sequences. Crystal structures of the TRAF domain of human TRAF2 in complex with peptides from the TNFR family members CD40, CD30, Ox40, 4-1BB, and the EBV oncoprotein LMP1 revealed a conserved binding mode. A major TRAF2-binding consensus sequence, (P/S/A/T)x(Q/E)E, and a minor consensus motif, PxQxxD, can be defined from the structural analysis, which encompass all known TRAF2-binding sequences. The structural information provides a template for the further dissection of receptor binding specificity of TRAF2 and for the understanding of the complexity of TRAF-mediated signal transduction.

PubMed: 10518213
DOI: 10.1016/S1097-2765(00)80334-2

実験手法

X-RAY DIFFRACTION (2.5 Å)