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Title
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Interaction of the NK cell inhibitory receptor Ly49A with H-2Dd: identification of a site distinct from the TCR site.
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Authors
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K.Natarajan,
L.F.Boyd,
P.Schuck,
W.M.Yokoyama,
D.Eliat,
D.H.Margulies.
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Ref.
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Immunity, 1999,
11,
591-601.
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PubMed id
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Abstract
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Natural killer cell function is controlled by interaction of NK receptors with
MHC I molecules expressed on target cells. We describe the binding of
bacterially expressed Ly49A, the prototype murine NK inhibitory receptor, to
similarly engineered H-2Dd. Despite its homology to C-type lectins, Ly49A binds
independently of carbohydrate and Ca2+ and shows specificity for MHC I but not
bound peptide. The affinity of the Ly49A/H-2Dd interaction as determined by
surface plasmon resonance is from 6 to 26 microM at 25 degrees C and is greater
by ultracentrifugation at 4 degrees C. Biotinylated Ly49A stains
H-2Dd-expressing cells. Competition experiments indicate that the Ly49A and T
cell receptor (TCR) binding sites on MHC I are distinct, suggesting complex
regulation of cells that bear both TCR and NK cell receptors.
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