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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6762
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pubmed:dateCreated |
2000-1-4
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pubmed:databankReference |
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pubmed:abstractText |
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-2D(d) 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-2D(d). The Ly49A dimer interacts extensively with two H-2D(d) 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-2D(d) alpha2 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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Ly,
http://linkedlifedata.com/resource/pubmed/chemical/H-2 Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, NK Cell Lectin-Like,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/histocompatibility antigen H-2D(b)
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
402
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
623-31
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10604468-Antigens, Ly,
pubmed-meshheading:10604468-Crystallography, X-Ray,
pubmed-meshheading:10604468-Escherichia coli,
pubmed-meshheading:10604468-H-2 Antigens,
pubmed-meshheading:10604468-Humans,
pubmed-meshheading:10604468-Killer Cells, Natural,
pubmed-meshheading:10604468-Lectins, C-Type,
pubmed-meshheading:10604468-Macromolecular Substances,
pubmed-meshheading:10604468-Models, Molecular,
pubmed-meshheading:10604468-Molecular Sequence Data,
pubmed-meshheading:10604468-Protein Binding,
pubmed-meshheading:10604468-Protein Conformation,
pubmed-meshheading:10604468-Protein Folding,
pubmed-meshheading:10604468-Receptors, Immunologic,
pubmed-meshheading:10604468-Receptors, NK Cell Lectin-Like,
pubmed-meshheading:10604468-Recombinant Proteins,
pubmed-meshheading:10604468-Sequence Alignment,
pubmed-meshheading:10604468-Signal Transduction
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pubmed:year |
1999
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pubmed:articleTitle |
Crystal structure of a lectin-like natural killer cell receptor bound to its MHC class I ligand.
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pubmed:affiliation |
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville 20850, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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