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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1995-7-5
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pubmed:abstractText |
The adaptive immune system is capable of responding to an infinite number of antigens with the antigen-specific receptors immunoglobulin (Ig) and the T cell receptor (TCR). Ig binds soluble antigens while TCR recognizes antigen bound in clefts of polymorphic self-encoded major histocompatibility complex (MHC) class I and class II molecules. All of these molecules are wholly or partially composed of Ig superfamily domains. TCR and Ig use V-set Ig superfamily domains, always in heterodimeric forms, in antigen recognition. Although the ways in which TCR and Ig bind antigen are fundamentally different, the structure of the heterodimeric V domains is probably identical. The antigen-binding cleft of MHC proteins has a structure unlike Ig superfamily domains, although several investigators have proposed that this cleft is evolutionarily derived from Ig domains. We believe the MHC cleft is a primitive structure, perhaps related to the peptide-binding domains of intracellular chaperone proteins. A model is proposed whereby chaperone proteins were the primordial MHC molecules, presenting peptides derived from invariant proteins residing inside cells for recognition by lymphocytes with minimally diverse receptors. Such a system may be reflected today by the epithelial immune system, apparently governed by monomorphic MHC molecules and lymphocytes with unconventional antigen-specific receptors.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0300-5208
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
186
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
224-32; discussion 233-6
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:7768153-Adaptation, Physiological,
pubmed-meshheading:7768153-Animals,
pubmed-meshheading:7768153-Biological Evolution,
pubmed-meshheading:7768153-Humans,
pubmed-meshheading:7768153-Immunoglobulins,
pubmed-meshheading:7768153-Major Histocompatibility Complex,
pubmed-meshheading:7768153-Receptors, Antigen, T-Cell,
pubmed-meshheading:7768153-Vertebrates
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pubmed:year |
1994
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pubmed:articleTitle |
Primitive vertebrate immunity: what is the evolutionary derivative of molecules that define the adaptive immune system?
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pubmed:affiliation |
Department of Microbiology and Immunology, University of Miami, FL 33136, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
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