2AW2

Crystal structure of the human BTLA-HVEM complex

2AW2 の概要

• エントリーDOI: 10.2210/pdb2aw2/pdb
• 関連するPDBエントリー: 1JMA 1XAU
• 分子名称: B and T lymphocyte attenuator, Tumor necrosis factor receptor superfamily member 14, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: igi domain, igg domain, tnfrsf, protein-protein complex, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 51956.29

構造登録者

Compaan, D.M.,Gonzalez, L.C.,Tom, I.,Loyet, K.M.,Eaton, D.,Hymowitz, S.G. (登録日: 2005-08-31, 公開日: 2005-09-27, 最終更新日: 2024-10-30)

主引用文献

Compaan, D.M.,Gonzalez, L.C.,Tom, I.,Loyet, K.M.,Eaton, D.,Hymowitz, S.G.
Attenuating Lymphocyte Activity: the crystal structure of the BTLA-HVEM complex
J.Biol.Chem., 280:39553-39561, 2005

PubMed Abstract: Five CD28-like proteins exert positive or negative effects on immune cells. Only four of these five receptors interact with members of the B7 family. The exception is BTLA (B and T lymphocyte attenuator), which instead interacts with the tumor necrosis factor receptor superfamily member HVEM (herpes virus entry mediator). To better understand this interaction, we determined the 2.8-A crystal structure of the BTLA-HVEM complex. This structure shows that BTLA binds the N-terminal cysteine-rich domain of HVEM and employs a unique binding surface compared with other CD28-like receptors. Moreover, the structure shows that BTLA recognizes the same surface on HVEM as gD (herpes virus glycoprotein D) and utilizes a similar binding motif. Light scattering analysis demonstrates that the extracellular domain of BTLA is monomeric and that BTLA and HVEM form a 1:1 complex. Alanine-scanning mutagenesis of HVEM was used to further define critical binding residues. Finally, BTLA adopts an immunoglobulin I-set fold. Despite structural similarities to other CD28-like members, BTLA represents a unique co-receptor.

PubMed: 16169851
DOI: 10.1074/jbc.M507629200

実験手法

X-RAY DIFFRACTION (2.8 Å)