4BFG
Structure of the extracellular portion of mouse CD200R
4BFG の概要
| エントリーDOI | 10.2210/pdb4bfg/pdb |
| 関連するPDBエントリー | 4BFE 4BFI |
| 分子名称 | CELL SURFACE GLYCOPROTEIN CD200 RECEPTOR 1, 2-acetamido-2-deoxy-beta-D-glucopyranose, ACETATE ION, ... (6 entities in total) |
| 機能のキーワード | immune system, paired receptor, ig domains, viral mimicry, leukaemia |
| 由来する生物種 | MUS MUSCULUS (HOUSE MOUSE) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 24531.15 |
| 構造登録者 | Hatherley, D.,Lea, S.M.,Johnson, S.,Barclay, A.N. (登録日: 2013-03-18, 公開日: 2013-05-01, 最終更新日: 2024-10-16) |
| 主引用文献 | Hatherley, D.,Lea, S.M.,Johnson, S.,Barclay, A.N. Structures of Cd200/Cd200 Receptor Family and Implications for Topology, Regulation, and Evolution Structure, 21:820-, 2013 Cited by PubMed Abstract: CD200 is a widely distributed membrane glycoprotein that regulates myeloid cell activity through its interaction with an inhibitory receptor (CD200R). The interaction is of interest as a target for treating excessive inflammation and for treating leukemia. There are closely related proteins to CD200R that give activating signals making this a "paired receptor." We report X-ray crystallography structures for the inhibitory CD200R, the activating receptor CD200RLa, and a complex between CD200R and CD200. Both CD200 and CD200R contain two Ig-like domains and interact through their NH₂ terminal domains compatible with immunological synapse-like interactions occurring between myeloid cells and other CD200-expressing cells. The failure of the activating receptor to bind CD200 resides in subtle changes around the interface. CD200 has been acquired by herpes viruses to mimic the host interaction. CD200R has evolved rapidly presumably driven by pathogen pressure but it may also be important in homeostasis through interactions with commensal bacteria. PubMed: 23602662DOI: 10.1016/J.STR.2013.03.008 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.08 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






