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natural killer (NK) cells are regulated by the interaction of Ly49 receptors with major histocompatibility complex class I molecules (MHC-I). Although the ligands for inhibitory Ly49 were considered to be restricted to classical MHC (MHC-Ia), we have shown that the non-classical MHC molecule (MHC-Ib) H2-M3 was a ligand for the inhibitory Ly49A. Here we establish that another MHC-Ib, H2-Q10, is a bona fide ligand for the inhibitory Ly49C receptor. H2-Q10 bound to Ly49C with a marginally lower affinity (\u223c5 \u03bcm) than that observed between Ly49C and MHC-Ia (H-2K(b)/H-2D(d), both \u223c1 \u03bcm), and this recognition could be prevented by cis interactions with H-2K in situ To understand the molecular details underpinning Ly49\u00b7MHC-Ib recognition, we determined the crystal structures of H2-Q10 and Ly49C bound H2-Q10. Unliganded H2-Q10 adopted a classical MHC-I fold and possessed a peptide-binding groove that exhibited features similar to those found in MHC-Ia, explaining the diverse peptide binding repertoire of H2-Q10. Ly49C bound to H2-Q10 underneath the peptide binding platform to a region that encompassed residues from the \u03b11, \u03b12, and \u03b13 domains, as well as the associated \u03b22-microglobulin subunit. This docking mode was conserved with that previously observed for Ly49C\u00b7H-2K(b) Indeed, structure-guided mutation of Ly49C indicated that Ly49C\u00b7H2-Q10 and Ly49C\u00b7H-2K(b) possess similar energetic footprints focused around residues located within the Ly49C \u03b24-stand and L5 loop, which contact the underside of the peptide-binding platform floor. Our data provide a structural basis for Ly49\u00b7MHC-Ib recognition and demonstrate that MHC-Ib represent an extended family of ligands for Ly49 molecules.","bibjson":{"author":[{"initials":"LC","lastname":"Sullivan","name":"Sullivan LC"},{"initials":"R","lastname":"Berry","name":"Berry R"},{"initials":"N","lastname":"Sosnin","name":"Sosnin N"},{"initials":"JM","lastname":"Widjaja","name":"Widjaja JM"},{"initials":"FA","lastname":"Deuss","name":"Deuss FA"},{"initials":"GR","lastname":"Balaji","name":"Balaji GR"},{"initials":"NL","lastname":"LaGruta","name":"LaGruta NL"},{"initials":"M","lastname":"Mirams","name":"Mirams M"},{"initials":"JA","lastname":"Trapani","name":"Trapani JA"},{"initials":"J","lastname":"Rossjohn","name":"Rossjohn J"},{"initials":"AG","lastname":"Brooks","name":"Brooks AG"},{"initials":"DM","lastname":"Andrews","name":"Andrews DM"}],"identifier":[{"id":"10.1074/jbc.m116.737130","type":"doi"},{"id":"27385590","type":"pubmed"}],"issue":[null],"journal":{"iso_abbreviation":"J. Biol. Chem.","name":""},"pages":[null],"title":"Recognition of the MHC class Ib molecule H2-Q10 by the natural killer cell receptor Ly49C.","type":"article","url":"https://www.sciencedirect.com/science/article/abs/pii/S0021925820307729","volume":[null],"year":[2016]},"in_pmc":"N","in_pmce":"Y","open_access":"N"},"resolution":"2.30","same_as":{"pdbe":{"url":"https://www.ebi.ac.uk/pdbe/entry/pdb/5j6h"},"rcsb":{"url":"https://www.rcsb.org/structure/5j6h"}},"species":{"common_name":"Mouse","match_type":"histo:assign_species","scientific_name":"Mus musculus","slug":"mus_musculus"},"tcr":null,"title":"H2-Q10 binding \"VGITNVDL\" at 2.30Å resolution","unique_chain_count":3}}