Human natural killer cell inhibitory receptors bind to HLA class I molecules.
To obtain direct evidence that human natural killer cell (NK) inhibitory receptors physically interact with polymorphic determinants of major histocompatibility complex class I molecules, a receptor termed NK-associated transcript-2 has been produced as a soluble fusion protein with the human IgG1 Fc portion. This soluble receptor binds specifically to HLA-C alleles with serine 77 and asparagine 80 in cell adhesion assays.
Döhring
C
C
Basel Institute for Immunology, Switzerland.
Colonna
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M
D000483:Alleles; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites / Q000276:immunology; D002460:Cell Line; D002461:Cell Line, Transformed; D005260:Female; D015235:HLA-B Antigens / Q000235:genetics; D015236:HLA-C Antigens / Q000235:genetics; D015395:Histocompatibility Antigens Class I / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D007694:Killer Cells, Natural / Q000737:chemistry / Q000378:metabolism*; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D011971:Receptors, Immunologic / Q000096:biosynthesis / Q000378:metabolism*; D054340:Receptors, KIR
D015235:HLA-B Antigens; D015236:HLA-C Antigens; D015395:Histocompatibility Antigens Class I; D011971:Receptors, Immunologic; D054340:Receptors, KIR