| http://purl.uniprot.org/citations/21335486 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21335486 | http://www.w3.org/2000/01/rdf-schema#comment | "NK cells become functionally competent to be triggered by their activation receptors through the interaction of NK cell inhibitory receptors with their cognate self-MHC ligands, an MHC-dependent educational process termed "licensing." For example, Ly49A(+) NK cells become licensed by the interaction of the Ly49A inhibitory receptor with its MHC class I ligand, H2D(d), whereas Ly49C(+) NK cells are licensed by H2K(b). Structural studies indicate that the Ly49A inhibitory receptor may interact with two sites, termed site 1 and site 2, on its H2D(d) ligand. Site 2 encompasses the α1/α2/α3 domains of the H2D(d) H chain and β(2)-microglobulin (β2m) and is the functional binding site for Ly49A in effector inhibition. Ly49C functionally interacts with a similar site in H2K(b). However, it is currently unknown whether this same site is involved in Ly49A- or Ly49C-dependent licensing. In this study, we produced transgenic C57BL/6 mice expressing wild-type or site 2 mutant H2D(d) molecules and studied whether Ly49A(+) NK cells are licensed. We also investigated Ly49A- and Ly49C-dependent NK licensing in murine β2m-deficient mice that are transgenic for human β2m, which has species-specific amino acid substitutions in β2m. Our data from these transgenic mice indicate that site 2 on self-MHC is critical for Ly49A- and Ly49C-dependent NK cell licensing. Thus, NK cell licensing through Ly49 involves specific interactions with its MHC ligand that are similar to those involved in effector inhibition."xsd:string |
| http://purl.uniprot.org/citations/21335486 | http://purl.org/dc/terms/identifier | "doi:10.4049/jimmunol.1004168"xsd:string |
| http://purl.uniprot.org/citations/21335486 | http://purl.uniprot.org/core/author | "Matsumoto N."xsd:string |
| http://purl.uniprot.org/citations/21335486 | http://purl.uniprot.org/core/author | "Choi T."xsd:string |
| http://purl.uniprot.org/citations/21335486 | http://purl.uniprot.org/core/author | "Yokoyama W.M."xsd:string |
| http://purl.uniprot.org/citations/21335486 | http://purl.uniprot.org/core/author | "Poursine-Laurent J."xsd:string |
| http://purl.uniprot.org/citations/21335486 | http://purl.uniprot.org/core/author | "Ferris S.T."xsd:string |
| http://purl.uniprot.org/citations/21335486 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21335486 | http://purl.uniprot.org/core/name | "J Immunol"xsd:string |
| http://purl.uniprot.org/citations/21335486 | http://purl.uniprot.org/core/pages | "3911-3917"xsd:string |
| http://purl.uniprot.org/citations/21335486 | http://purl.uniprot.org/core/title | "Ly49-dependent NK cell licensing and effector inhibition involve the same interaction site on MHC ligands."xsd:string |
| http://purl.uniprot.org/citations/21335486 | http://purl.uniprot.org/core/volume | "186"xsd:string |
| http://purl.uniprot.org/citations/21335486 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21335486 |
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