1D0G

CRYSTAL STRUCTURE OF DEATH RECEPTOR 5 (DR5) BOUND TO APO2L/TRAIL

1D0G の概要

• エントリーDOI: 10.2210/pdb1d0g/pdb
• 分子名称: DEATH RECEPTOR-5, APOPTOSIS-2 LIGAND, ZINC ION, ... (5 entities in total)
• 機能のキーワード: apoptosis, binding and specificity, ligand-receptor complex, tnf receptor family
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Membrane ; Single-pass type II membrane protein : P50591; Membrane; Single-pass type I membrane protein: O14763
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 102398.38

構造登録者

Hymowitz, S.G.,Christinger, H.W.,Fuh, G.,O'Connell, M.P.,Kelley, R.F.,Ashkenazi, A.,de Vos, A.M. (登録日: 1999-09-09, 公開日: 1999-10-22, 最終更新日: 2024-10-16)

主引用文献

Hymowitz, S.G.,Christinger, H.W.,Fuh, G.,Ultsch, M.,O'Connell, M.,Kelley, R.F.,Ashkenazi, A.,de Vos, A.M.
Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5.
Mol.Cell, 4:563-571, 1999

PubMed Abstract: Formation of a complex between Apo2L (also called TRAIL) and its signaling receptors, DR4 and DR5, triggers apoptosis by inducing the oligomerization of intracellular death domains. We report the crystal structure of the complex between Apo2L and the ectodomain of DR5. The structure shows three elongated receptors snuggled into long crevices between pairs of monomers of the homotrimeric ligand. The interface is divided into two distinct patches, one near the bottom of the complex close to the receptor cell surface and one near the top. Both patches contain residues that are critical for high-affinity binding. A comparison to the structure of the lymphotoxin-receptor complex suggests general principles of binding and specificity for ligand recognition in the TNF receptor superfamily.

PubMed: 10549288
DOI: 10.1016/S1097-2765(00)80207-5

実験手法

X-RAY DIFFRACTION (2.4 Å)