3FF7

Structure of NK cell receptor KLRG1 bound to E-cadherin

3FF7 の概要

• エントリーDOI: 10.2210/pdb3ff7/pdb
• 関連するPDBエントリー: 3FF8 3FF9
• 分子名称: Epithelial cadherin, Killer cell lectin-like receptor subfamily G member 1, ACETIC ACID, ... (4 entities in total)
• 機能のキーワード: klrg1-cadherin complex, calcium, cell adhesion, cell junction, cell membrane, cleavage on pair of basic residues, disease mutation, glycoprotein, membrane, phosphoprotein, polymorphism, transmembrane, alternative splicing, lectin, receptor, signal-anchor, cell adhesion-immune system complex, cell adhesion/immune system
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell junction : P12830; Cell membrane ; Single-pass type II membrane protein : Q96E93
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 48254.45

構造登録者

Li, Y.,Mariuzza, R.A. (登録日: 2008-12-02, 公開日: 2009-07-28, 最終更新日: 2024-10-16)

主引用文献

Li, Y.,Hofmann, M.,Wang, Q.,Teng, L.,Chlewicki, L.K.,Pircher, H.,Mariuzza, R.A.
Structure of natural killer cell receptor KLRG1 bound to E-cadherin reveals basis for MHC-independent missing self recognition.
Immunity, 31:35-46, 2009

PubMed Abstract: The cytolytic activity of natural killer (NK) cells is regulated by inhibitory receptors that detect the absence of self molecules on target cells. Structural studies of missing self recognition have focused on NK receptors that bind MHC. However, NK cells also possess inhibitory receptors specific for non-MHC ligands, notably cadherins, which are downregulated in metastatic tumors. We determined the structure of killer cell lectin-like receptor G1 (KLRG1) in complex with E-cadherin. KLRG1 mediates missing self recognition by binding to a highly conserved site on classical cadherins, enabling it to monitor expression of several cadherins (E-, N-, and R-) on target cells. This site overlaps the site responsible for cell-cell adhesion but is distinct from the integrin alpha(E)beta(7) binding site. We propose that E-cadherin may coengage KLRG1 and alpha(E)beta(7) and that KLRG1 overcomes its exceptionally weak affinity for cadherins through multipoint attachment to target cells, resulting in inhibitory signaling.

PubMed: 19604491
DOI: 10.1016/j.immuni.2009.04.019

実験手法

X-RAY DIFFRACTION (1.8 Å)