Source:http://linkedlifedata.com/resource/pubmed/id/12022472
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2002-5-22
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pubmed:abstractText |
This review, regards the low-affinity receptor CD23 as a C-type lectin and compares it with other C-type lectins and C-type lectin-like receptors. C-type lectins such as the asialoglycoprotein receptor, as well as the dendritic cell immunoreceptor and the dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin on dendritic cell lectin, possess amino acid sequences which interact with Ca++ and sugar, and many of them possess an endocytosis signal sequence that includes tyrosine or serine in the cytoplasmic region. In contrast, natural killer receptors lack the Ca++ and sugar-binding amino acids but conserve homologous cysteines in the form of C-type lectin, and possess an immunoreceptor tyrosine-based inhibitory motif in the cytoplasmic region which inhibits killer activity when they recognize the self major histocompatibility (MHC) class I molecule. Since human CD23a form has a similar amino acid sequence, the possibility that this sequence is an endocytosis signal or an ITIM is discussed. The function of the reverse RGD and RGD-binding inhibitory peptide in human CD23 from the point of view of the relation between a C-type lectin and MHC class II molecules is also considered.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin E,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fc,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, IgE,
http://linkedlifedata.com/resource/pubmed/chemical/arginyl-glycyl-aspartic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1420-682X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
59
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
648-64
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12022472-Amino Acid Sequence,
pubmed-meshheading:12022472-Animals,
pubmed-meshheading:12022472-Humans,
pubmed-meshheading:12022472-Immunoglobulin E,
pubmed-meshheading:12022472-Lectins,
pubmed-meshheading:12022472-Lectins, C-Type,
pubmed-meshheading:12022472-Leucine Zippers,
pubmed-meshheading:12022472-Ligands,
pubmed-meshheading:12022472-Models, Molecular,
pubmed-meshheading:12022472-Molecular Sequence Data,
pubmed-meshheading:12022472-Oligopeptides,
pubmed-meshheading:12022472-Protein Structure, Tertiary,
pubmed-meshheading:12022472-Receptors, Fc,
pubmed-meshheading:12022472-Receptors, IgE,
pubmed-meshheading:12022472-Sequence Alignment
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pubmed:year |
2002
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pubmed:articleTitle |
CD23 (the low-affinity IgE receptor) as a C-type lectin: a multidomain and multifunctional molecule.
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pubmed:affiliation |
Institute of Immunology, Hokkaido University, Sapporo, Japan. chk30950@hkg.odn.ne.jp
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pubmed:publicationType |
Journal Article,
Comparative Study,
Review
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