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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

DOI

10.1002/eji.200425089

Type

Journal article

Journal

European journal of immunology

Publication Date

06/2004

Volume

34

Pages

1673 - 1679

Addresses

Faculty of Medicine, King Chulalongkorn Memorial Hospital, Chulalongkorn University, Bangkok, Thailand.

Keywords

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