6NG3

Crystal structure of human CD160 and HVEM complex

6NG3 の概要

• エントリーDOI: 10.2210/pdb6ng3/pdb
• 分子名称: CD160 antigen,Tumor necrosis factor receptor superfamily member 14, beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: cd160, hvem, btla, gd, immune system
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27512.07

構造登録者

Liu, W.,Bonanno, J.,Almo, S.C. (登録日: 2018-12-21, 公開日: 2019-07-03, 最終更新日: 2024-10-30)

主引用文献

Liu, W.,Garrett, S.C.,Fedorov, E.V.,Ramagopal, U.A.,Garforth, S.J.,Bonanno, J.B.,Almo, S.C.
Structural Basis of CD160:HVEM Recognition.
Structure, 27:1286-1295.e4, 2019

PubMed Abstract: CD160 is a signaling molecule that interacts with herpes virus entry mediator (HVEM) and contributes to a wide range of immune responses, including T cell inhibition, natural killer cell activation, and mucosal immunity. GPI-anchored and transmembrane isoforms of CD160 share the same ectodomain responsible for HVEM engagement, which leads to bidirectional signaling. Despite the importance of the CD160:HVEM signaling axis and its therapeutic relevance, the structural and mechanistic basis underlying CD160-HVEM engagement has not been described. We report the crystal structures of the human CD160 extracellular domain and its complex with human HVEM. CD160 adopts a unique variation of the immunoglobulin fold and exists as a monomer in solution. The CD160:HVEM assembly exhibits a 1:1 stoichiometry and a binding interface similar to that observed in the BTLA:HVEM complex. Our work reveals the chemical and physical determinants underlying CD160:HVEM recognition and initiation of associated signaling processes.

PubMed: 31230945
DOI: 10.1016/j.str.2019.05.010

実験手法

X-RAY DIFFRACTION (2.88 Å)