2HEY

Crystal structure of murine OX40L bound to human OX40

2HEY の概要

• エントリーDOI: 10.2210/pdb2hey/pdb
• 関連するPDBエントリー: 2hev 2hew
• 分子名称: Tumor necrosis factor ligand superfamily member 4, Tumor necrosis factor receptor superfamily member 4, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: cytokine, receptor-ligan complex, co-stimulator, tnfsf
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Membrane; Single-pass type II membrane protein: P43488; Membrane; Single-pass type I membrane protein: P43489
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 65842.37

構造登録者

Hymowitz, S.G. (登録日: 2006-06-22, 公開日: 2006-08-29, 最終更新日: 2024-11-20)

主引用文献

Compaan, D.M.,Hymowitz, S.G.
The Crystal Structure of the Costimulatory OX40-OX40L Complex.
Structure, 14:1321-1330, 2006

PubMed Abstract: OX40 is a T cell costimulator activated by OX40L. Blockade of the OX40L-OX40 interaction has ameliorative effects in animal models of T cell pathologies. In order to better understand the interaction between OX40 and OX40L, we have determined the crystal structure of murine OX40L and of the human OX40-OX40L complex at 1.45 and 2.4 A, respectively. These structures show that OX40L is an unusually small member of the tumor necrosis factor superfamily (TNFSF). The arrangement of the OX40L protomers forming the functional trimer is atypical and differs from that of other members by a 15 degrees rotation of each protomer with respect to the trimer axis, resulting in an open assembly. Site-directed changes of the interfacial residues of OX40L suggest this interface lacks a single "hot spot" and that instead, binding energy is dispersed over at least two distinct areas. These structures demonstrate the structural plasticity of TNFSF members and their interactions with receptors.

PubMed: 16905106
DOI: 10.1016/j.str.2006.06.015

実験手法

X-RAY DIFFRACTION (2 Å)