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10.1074/jbc.M116.737130 http://scihub22266oqcxt.onion/10.1074/jbc.M116.737130 C5009249!5009249 !27385590     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27385590 &cmd=llinks): Failed to open stream: HTTP request failed! 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Recognition of the Major Histocompatibility Complex (MHC) Class Ib Molecule H2-Q10 by the Natural Killer Cell Receptor Ly49C |pdf=|usr=}}{{27385590 }} gab.com Text Recognition of the Major Histocompatibility Complex (MHC) Class Ib Molecule H2-Q10 by the Natural Killer Cell Receptor Ly49C JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=27385590 #FOAvip Murine 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 (?5 ?m) than that observed between Ly49C and MHC-Ia (H-2K(b)/H-2D(d), both ?1 ?m), and this recognition could be prevented by cis interactions with H-2K in situ To understand the molecular details underpinning Ly49·MHC-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 ?1, ?2, and ?3 domains, as well as the associated ?2-microglobulin subunit. This docking mode was conserved with that previously observed for Ly49C·H-2K(b) Indeed, structure-guided mutation of Ly49C indicated that Ly49C·H2-Q10 and Ly49C·H-2K(b) possess similar energetic footprints focused around residues located within the Ly49C ?4-stand and L5 loop, which contact the underside of the peptide-binding platform floor. Our data provide a structural basis for Ly49·MHC-Ib recognition and demonstrate that MHC-Ib represent an extended family of ligands for Ly49 molecules. Twit Text FOAVip Recognition of the Major Histocompatibility Complex (MHC) Class Ib Molecule H2-Q10 by the Natural Killer Cell Receptor Ly49C ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=27385590 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27385590 #FOAvip English Wikipedia <ref>{{Cite pmid|27385590 }}</ref> Recognition of the Major Histocompatibility Complex (MHC) Class Ib Molecule H2-Q10 by the Natural Killer Cell Receptor Ly49C #MMPMID27385590 Sullivan LC ; Berry R ; Sosnin N ; Widjaja JM ; Deuss FA ; Balaji GR ; LaGruta NL ; Mirams M ; Trapani JA ; Rossjohn J ; Brooks AG ; Andrews DM J Biol Chem 2016[Sep]; 291 (36 ): 18740-52 PMID27385590 show ga Murine 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 (?5 ?m) than that observed between Ly49C and MHC-Ia (H-2K(b)/H-2D(d), both ?1 ?m), and this recognition could be prevented by cis interactions with H-2K in situ To understand the molecular details underpinning Ly49·MHC-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 ?1, ?2, and ?3 domains, as well as the associated ?2-microglobulin subunit. This docking mode was conserved with that previously observed for Ly49C·H-2K(b) Indeed, structure-guided mutation of Ly49C indicated that Ly49C·H2-Q10 and Ly49C·H-2K(b) possess similar energetic footprints focused around residues located within the Ly49C ?4-stand and L5 loop, which contact the underside of the peptide-binding platform floor. Our data provide a structural basis for Ly49·MHC-Ib recognition and demonstrate that MHC-Ib represent an extended family of ligands for Ly49 molecules. |Animals [MESH] |Crystallography, X-Ray [MESH] |H-2 Antigens/chemistry/genetics/immunology [MESH] |Histocompatibility Antigen H-2D/*chemistry/genetics/immunology [MESH] |Killer Cells, Natural/*chemistry/immunology [MESH] |Mice [MESH] |Mice, Knockout [MESH] |NK Cell Lectin-Like Receptor Subfamily A/*chemistry/genetics/immunology [MESH] |Protein Domains [MESH]Recognition of the Major Histocompatibility Complex (MHC) Class Ib Mol(epmc).pdf DeepDyve Pubget Overpricing