1DU3

Crystal structure of TRAIL-SDR5

1DU3 の概要

• エントリーDOI: 10.2210/pdb1du3/pdb
• 関連するPDBエントリー: 1D0G 1D4V
• 分子名称: DEATH RECEPTOR 5, TNF-RELATED APOPTOSIS INDUCING LIGAND, ZINC ION, ... (4 entities in total)
• 機能のキーワード: trail, dr5, complex, apoptosis
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: O14763; Membrane ; Single-pass type II membrane protein : P50591
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 204725.85

構造登録者

Cha, S.-S.,Sung, B.-J.,Oh, B.-H. (登録日: 2000-01-14, 公開日: 2000-09-27, 最終更新日: 2024-11-06)

主引用文献

Cha, S.-S.,Sung, B.-J.,Kim, Y.A.,Song, Y.L.,Kim, H.J.,Kim, S.,Lee, M.S.,Oh, B.-H.
Crystal structure of TRAIL-DR5 complex identifies a critical role of the unique frame insertion in conferring recognition specificity
J.Biol.Chem., 275:31171-31177, 2000

PubMed Abstract: TRAIL is a cytokine that induces apoptosis in a wide variety of tumor cells but rarely in normal cells. It contains an extraordinarily elongated loop because of an unique insertion of 12-16 amino acids compared with the other members of tumor necrosis factor family. Biological implication of the frame insertion has not been clarified. We have determined the crystal structure of TRAIL in a complex with the extracellular domain of death receptor DR5 at 2.2 A resolution. The structure reveals extensive contacts between the elongated loop and DR5 in an interaction mode that would not be allowed without the frame insertion. These interactions are missing in the structures of the complex determined by others recently. This observation, along with structure-inspired deletion analysis, identifies the critical role of the frame insertion as a molecular strategy conferring specificity upon the recognition of cognate receptors. The structure also suggests that a built-in flexibility of the tumor necrosis factor receptor family members is likely to play a general and important role in the binding and recognition of tumor necrosis factor family members.

PubMed: 10893238
DOI: 10.1074/jbc.M004414200

実験手法

X-RAY DIFFRACTION (2.2 Å)