3FF8
Structure of NK cell receptor KLRG1 bound to E-cadherin
Summary for 3FF8
| Entry DOI | 10.2210/pdb3ff8/pdb |
| Related | 3FF7 3FF9 |
| Descriptor | Epithelial cadherin, Killer cell lectin-like receptor subfamily G member 1, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | klrg1-cadherin complex, calcium, cell adhesion, cell junction, cell membrane, cleavage on pair of basic residues, disease mutation, glycoprotein, membrane, phosphoprotein, polymorphism, transmembrane, lectin, receptor, signal-anchor, cell adhesion-immune system complex, cell adhesion/immune system |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cell junction : P12830 Cell membrane ; Single-pass type II membrane protein : O88713 |
| Total number of polymer chains | 4 |
| Total formula weight | 48901.88 |
| Authors | Li, Y.,Mariuzza, R.A. (deposition date: 2008-12-02, release date: 2009-07-28, Last modification date: 2023-09-06) |
| Primary citation | 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 Cited by 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: 19604491DOI: 10.1016/j.immuni.2009.04.019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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