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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2000-1-4
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pubmed:abstractText |
LIR-1 is a class I MHC receptor related to natural killer inhibitory receptors (KIRs). Binding of LIR-1 or KIRs to class I molecules results in inhibitory signals. Unlike individual KIRs, LIR-1 recognizes many class I alleles and also binds UL18, a human cytomegalovirus class I MHC homolog. Here, we show that LIR-1 interacts with the relatively nonpolymorphic alpha3 domain of class I proteins and the analogous region of UL18 using its N-terminal immunoglobulin-like domain. The >1000-fold higher affinity of LIR-1 for UL18 than for class I illustrates how a viral protein competes with host proteins to subvert the host immune response. LIR-1 recognition of class I molecules resembles the CD4-class II MHC interaction more than the KIR-class I interaction, implying a functional distinction between LIR-1 and KIRs.
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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, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Capsid Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class I,
http://linkedlifedata.com/resource/pubmed/chemical/LILRB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, KIR,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/VP23 protein, Human herpesvirus 1,
http://linkedlifedata.com/resource/pubmed/chemical/beta 2-Microglobulin
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1074-7613
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
603-13
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10591185-Alleles,
pubmed-meshheading:10591185-Animals,
pubmed-meshheading:10591185-Antigens, CD,
pubmed-meshheading:10591185-CHO Cells,
pubmed-meshheading:10591185-Capsid,
pubmed-meshheading:10591185-Capsid Proteins,
pubmed-meshheading:10591185-Cricetinae,
pubmed-meshheading:10591185-Cricetulus,
pubmed-meshheading:10591185-Cytomegalovirus,
pubmed-meshheading:10591185-Glycosylation,
pubmed-meshheading:10591185-Histocompatibility Antigens Class I,
pubmed-meshheading:10591185-Humans,
pubmed-meshheading:10591185-Killer Cells, Natural,
pubmed-meshheading:10591185-Macromolecular Substances,
pubmed-meshheading:10591185-Models, Molecular,
pubmed-meshheading:10591185-Protein Binding,
pubmed-meshheading:10591185-Protein Denaturation,
pubmed-meshheading:10591185-Protein Folding,
pubmed-meshheading:10591185-Protein Processing, Post-Translational,
pubmed-meshheading:10591185-Protein Structure, Tertiary,
pubmed-meshheading:10591185-Receptors, Immunologic,
pubmed-meshheading:10591185-Receptors, KIR,
pubmed-meshheading:10591185-Recombinant Fusion Proteins,
pubmed-meshheading:10591185-Solubility,
pubmed-meshheading:10591185-Transfection,
pubmed-meshheading:10591185-beta 2-Microglobulin
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pubmed:year |
1999
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pubmed:articleTitle |
The inhibitory receptor LIR-1 uses a common binding interaction to recognize class I MHC molecules and the viral homolog UL18.
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pubmed:affiliation |
Graduate Option in Biochemistry, Howard Hughes Medical Institute, California Institute of Technology, Pasadena 91125, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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