The Journal of Experimental Medicine
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Published online 31 March 2003 doi:10.1084/jem.20021624
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© Rockefeller University Press, 0022-1007/2003/4/933 $5.00
The Journal of Experimental Medicine, Volume 197, Number 7, 933-938

Brief Definitive Report

 Crystal Structure of the Human Natural Killer Cell Activating Receptor KIR2DS2 (CD158j)

Xavier Saulquin1, Louis N. Gastinel2 and Eric Vivier1

1 Centre d'Immunologie de Marseille-Luminy, Centre National de la Recherche Scientifique (CNRS)–Institut National de la Santé et de la Recherche Médicale (INSERM)–Université de la Méditerranée, Campus de Luminy, Case 906, 13288 Marseille Cedex 09, France
2 Architecture et Fonction des Macromolecules Biologiques, CNRS UMR 6098, 13402 Marseille Cedex 20, France

Address correspondence to Eric Vivier, Centre d'Immunologie INSERM-CNRS, de Marseille Luminy, Case 906, Parc Scientifique de Luminy, Marseille Cedex 09, 13288 France. Phone: 33-4-91-26-94-44; Fax: 33-4-91-26-94-30; E-mail: vivier{at}ciml.univ-mrs.fr; or Louis N. Gastinel at his present address, Institut des Sciences de la Vie et de la Santé, UMR 1061, Institut National de la Recherche Agronomique, Université de Limoges, Faculté des Sciences, 123 Avenue Albert Thomas, 87060 Limoges Cedex, France. Phone: 33-0-5-55-45-76-60; Fax: 33-0-5-55-45-76-53; E-mail: lgastinel{at}unilim.fr

Killer cell Ig-like receptors (KIRs) regulate the function of human natural killer and T cell subsets. A feature of the KIR locus is the clustering of homologous genes encoding for inhibitory and activating KIR. Inhibitory and activating KIR differ for ligand specificities and/or affinities. In particular, we show here with KIR tetramers that activating KIR2DS2 does not bind HLA-Cw3 molecules recognized by inhibitory KIR2DL2, despite 99% extracellular amino acid identity. We also report the 2.3-Å structure of KIR2DS2, which reveals subtle displacements of two residues (Tyr45 and Gln71) involved in the interaction of KIR2DL2 with HLA-Cw3. These results show that KIR molecules cannot tolerate any variability in their three-dimensional structure without altering their MHC class I recognition capacities. Therefore, the mode of recognition used by KIR largely differs from the conformational changes that characterize T cell receptor or NKG2D interaction with their respective ligands.

Key Words: KIR • crystal structure


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