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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0020204,
umls-concept:C0021467,
umls-concept:C0021469,
umls-concept:C0024518,
umls-concept:C0030956,
umls-concept:C0033684,
umls-concept:C0034790,
umls-concept:C0039194,
umls-concept:C0456387,
umls-concept:C0680844,
umls-concept:C0681916,
umls-concept:C0750572,
umls-concept:C1510827,
umls-concept:C1749467
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pubmed:issue |
1
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pubmed:dateCreated |
1989-2-23
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pubmed:abstractText |
To investigate the molecular basis of the interaction between the T cell receptor and the MHC class I antigen in an allogeneic response, a soluble counterpart of the murine class I molecule, H-2Kb, was genetically engineered. Cells secreting this soluble molecule, H-2Kb/Q10b, inhibited stimulation of an H-2Kb-reactive T cell hybridoma by cells transfected with H-2Kbm10, a weak stimulus, but not by H-2Kb- or H-2Kbm6-transfected cells. Soluble purified H-2Kb/Q10b protein also blocked T cell stimulation. In addition, a peptide from the wild-type H-2Kb molecule spanning the region of the bm10 mutation specifically inhibited activation of the T cell hybridoma by H-2Kbm10 cells, thus suggesting that amino acid residues 163-174 of H-2Kb define a region important for T cell receptor binding. An estimate for the Kd of the T cell receptor for soluble H-2Kb/Q10b was 10(-7) M, while the Kd for soluble peptide 163-174 was 10(-4) M.
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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:month |
Jan
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pubmed:issn |
0092-8674
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
56
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
47-55
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2783386-Animals,
pubmed-meshheading:2783386-H-2 Antigens,
pubmed-meshheading:2783386-L Cells (Cell Line),
pubmed-meshheading:2783386-Lymphocyte Activation,
pubmed-meshheading:2783386-Major Histocompatibility Complex,
pubmed-meshheading:2783386-Mice,
pubmed-meshheading:2783386-Peptides,
pubmed-meshheading:2783386-Receptors, Antigen, T-Cell,
pubmed-meshheading:2783386-Solubility,
pubmed-meshheading:2783386-Structure-Activity Relationship,
pubmed-meshheading:2783386-T-Lymphocytes,
pubmed-meshheading:2783386-Transfection
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pubmed:year |
1989
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pubmed:articleTitle |
Inhibition of an allospecific T cell hybridoma by soluble class I proteins and peptides: estimation of the affinity of a T cell receptor for MHC.
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pubmed:affiliation |
Molecular Biology Section, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892.
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pubmed:publicationType |
Journal Article,
In Vitro
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