Source:http://linkedlifedata.com/resource/pubmed/id/11955595
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
14
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pubmed:dateCreated |
2002-4-16
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pubmed:abstractText |
Natural killer (NK) cells function through a diverse array of cell-surface natural killer receptors (NCRs). NCRs specific for classical and non-classical MHC class I proteins, expressed in complex patterns of inhibitory and activating isoforms on overlapping, but distinct, subsets of NK cells, play an important role in immunosurveillance against cells that have reduced MHC class I expression as a result of infection or transformation. Another NCR, NKG2D, is an activating NCR first identified on NK cells, but subsequently found on macrophages and a variety of T cell types. NKG2D ligands in rodents include the MHC class I-like proteins RAE-1 and H60 and, in humans, ULBPs and the cell stress-inducible proteins MICA and MICB. NKG2D-MIC and -RAE-1 recognition events have been implicated in anti-viral and -tumor immune responses. Crystallographic analyses of NKG2D-MICA and -RAE-1 complexes reveal an unusual mode of recognition that apparently tolerates a surprising degree of ligand plasticity while generating affinities that are among the strongest TCR- or NCR-ligand affinities, thus, far described.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/KLRK1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/NK Cell Lectin-Like Receptor...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Natural Killer Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0161-5890
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
38
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1029-37
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11955595-Animals,
pubmed-meshheading:11955595-Binding Sites,
pubmed-meshheading:11955595-Dimerization,
pubmed-meshheading:11955595-Humans,
pubmed-meshheading:11955595-Killer Cells, Natural,
pubmed-meshheading:11955595-Ligands,
pubmed-meshheading:11955595-Lymphocyte Activation,
pubmed-meshheading:11955595-Models, Molecular,
pubmed-meshheading:11955595-NK Cell Lectin-Like Receptor Subfamily K,
pubmed-meshheading:11955595-Protein Structure, Tertiary,
pubmed-meshheading:11955595-Receptors, Immunologic,
pubmed-meshheading:11955595-Receptors, Natural Killer Cell,
pubmed-meshheading:11955595-Solutions
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pubmed:year |
2002
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pubmed:articleTitle |
Asymmetric ligand recognition by the activating natural killer cell receptor NKG2D, a symmetric homodimer.
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pubmed:affiliation |
Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA. rstrong@fhcrc.org
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
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