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	Eur. J. Immunol. May (2000); 30(5):1480-5
Definition of polymorphic residues on killer Ig-like receptor proteins which contribute to the HLA-C binding site.
Richardson J, Reyburn HT, Luque I, Vales-Gomez M, Strominger JL
Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
Abstract: Killer cell immunoglobulin-like receptors (KIR) bind HLA class I proteins in an allele- and locus-specific manner. This report describes the use of transfectants expressing recombinant chimeric proteins, comprising the extracellular portions of KIR molecules and the transmembrane and cytoplasmic tails of CD3-zeta, to create an in vitro system in which signaling is readily measured and that preserves the specificity of the KIR / HLA-C interaction. The identity of the amino acid residues on the KIR molecule important for binding to the HLA protein is not well understood; although some KIR2D residues involved in HLA-C recognition have been identified, their relative importance and whether other amino acids contribute to binding was unclear. This novel system was used to study, by site-directed mutagenesis, the role of various amino acids in KIR binding to HLA-C ligand. The data presented here show that while multiple polymorphic residues contribute to the HLA-C binding site on KIR proteins, two clusters of polymorphic residues define the group allotype specificity of HLA-C binding to a KIR2D molecule.
[PUBMED: 10820396]