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PDBsum entry 3ff9
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Immune system
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PDB id
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3ff9
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References listed in PDB file
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Key reference
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Title
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Structure of natural killer cell receptor klrg1 bound to e-Cadherin reveals basis for mhc-Independent missing self recognition.
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Authors
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Y.Li,
M.Hofmann,
Q.Wang,
L.Teng,
L.K.Chlewicki,
H.Pircher,
R.A.Mariuzza.
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Ref.
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Immunity, 2009,
31,
35-46.
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PubMed id
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Abstract
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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.
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