1D4V

Crystal structure of trail-DR5 complex

1D4V の概要

• エントリーDOI: 10.2210/pdb1d4v/pdb
• 分子名称: TNF-RELATED APOPTOSIS INDUCING LIGAND, DEATH RECEPTOR 5 (3 entities in total)
• 機能のキーワード: ligand-receptor complex, trimeric jelly-roll, tnf-r superfamily, apoptosis
• 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
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32064.83

構造登録者

Mongkolsapaya, J.,Grimes, J.M.,Stuart, D.I.,Jones, E.Y.,Screaton, G.R. (登録日: 1999-10-06, 公開日: 1999-11-01, 最終更新日: 2024-10-30)

主引用文献

Mongkolsapaya, J.,Grimes, J.M.,Chen, N.,Xu, X.N.,Stuart, D.I.,Jones, E.Y.,Screaton, G.R.
Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation
Nat.Struct.Biol., 6:1048-1053, 1999

PubMed Abstract: TRAIL, an apoptosis inducing ligand, has at least four cell surface receptors including the death receptor DR5. Here we report the crystal structure at 2.2 A resolution of a complex between TRAIL and the extracellular region of DR5. TRAIL forms a central homotrimer around which three DR5 molecules bind. Radical differences in the surface charge of the ligand, together with variation in the alignment of the two receptor domains confer specificity between members of these ligand and receptor families. The existence of a switch mechanism allowing variation in receptor domain alignment may mean that it is possible to engineer receptors with multiple specificities by exploiting contact positions unique to individual receptor-ligand pairs.

PubMed: 10542098
DOI: 10.1038/14935

実験手法

X-RAY DIFFRACTION (2.2 Å)