Crystal structure of an NK cell immunoglobulin-like receptor in complex with its class I MHC ligand

Jeffrey C. Boyington, Shawn A. Motyka, Peter Schuck, Andrew G. Brooks and Peter D. Sun ()
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Jeffrey C. Boyington: Structural Biology Section, Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Shawn A. Motyka: Biochemistry, Cellular and Molecular Biology Program, Johns Hopkins University School of Medicine
Peter Schuck: Bioengineering and Physical Science Program, National Institutes of Health
Andrew G. Brooks: Department of Microbiology and Immunology University of Melbourne
Peter D. Sun: Structural Biology Section, Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, National Institutes of Health

Nature, 2000, vol. 405, issue 6786, 537-543

Abstract: Abstract Target cell lysis is regulated by natural killer (NK) cell receptors that recognize class I MHC molecules. Here we report the crystal structure of the human immunoglobulin-like NK cell receptor KIR2DL2 in complex with its class I ligand HLA-Cw3 and peptide. KIR binds in a nearly orthogonal orientation across the α1 and α2 helices of Cw3 and directly contacts positions 7 and 8 of the peptide. No significant conformational changes in KIR occur on complex formation. The receptor footprint on HLA overlaps with but is distinct from that of the T-cell receptor. Charge complementarity dominates the KIR/HLA interface and mutations that disrupt interface salt bridges substantially diminish binding. Most contacts in the complex are between KIR and conserved HLA-C residues, but a hydrogen bond between Lys 44 of KIR2DL2 and Asn 80 of Cw3 confers the allotype specificity. KIR contact requires position 8 of the peptide to be a residue smaller than valine. A second KIR/HLA interface produced an ordered receptor–ligand aggregation in the crystal which may resemble receptor clustering during immune synapse formation.

Date: 2000
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DOI: 10.1038/35014520

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