Crystal structure of a lectin-like natural killer cell receptor bound to its MHC class I ligand

José Tormo, Kannan Natarajan, David H. Margulies () and Roy A. Mariuzza ()
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José Tormo: University of Maryland Biotechnology Institute
Kannan Natarajan: Molecular Biology Section, Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health
David H. Margulies: Molecular Biology Section, Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health
Roy A. Mariuzza: University of Maryland Biotechnology Institute

Nature, 1999, vol. 402, issue 6762, 623-631

Abstract: Abstract Natural killer (NK) cell function is regulated by NK receptors that interact with MHC class I (MHC-I) molecules on target cells. The murine NK receptor Ly49A inhibits NK cell activity by interacting with H-2Dd through its C-type-lectin-like NK receptor domain. Here we report the crystal structure of the complex between the Ly49A NK receptor domain and unglycosylated H-2Dd. The Ly49A dimer interacts extensively with two H-2Dd molecules at distinct sites. At one interface, a single Ly49A subunit contacts one side of the MHC-I peptide-binding platform, presenting an open cavity towards the conserved glycosylation site on the H-2Dd α2 domain. At a second, larger interface, the Ly49A dimer binds in a region overlapping the CD8-binding site. The smaller interface probably represents the interaction between Ly49A on the NK cell and MHC-I on the target cell, whereas the larger one suggests an interaction between Ly49A and MHC-I on the NK cell itself. Both Ly49A binding sites on MHC-I are spatially distinct from that of the T-cell receptor.

Date: 1999
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DOI: 10.1038/45170

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