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The recognition of MHC class I molecules by killer cell immunoglobulin-like receptors (KIR) is central to the control of NK cell function and can also modulate the CTL activation threshold. Among KIR receptors, KIR3DL2 is thought to interact with HLA-A3 and -A11, although direct evidence has been lacking. In this study, we show that HLA-A3 and -A11 tetramers specifically bind to KIR3DL2*001 transfectants and that this recognition is peptide-specific. Single amino acid substitutions in the nonamer peptide underline a critical role for residue 8 in recognition of KIR3DL2. However, the role of this interaction in vivo still remains to be established.

Original publication




Journal article


Eur J Immunol

Publication Date





1673 - 1679


Flow Cytometry, HLA-A Antigens, HLA-A11 Antigen, HLA-A3 Antigen, Humans, Killer Cells, Natural, Peptide Fragments, Protein Conformation, Receptors, Immunologic, Receptors, KIR, Receptors, KIR3DL2, T-Lymphocytes, Cytotoxic, Transfection