pubmed-article:7680688 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7680688 | lifeskim:mentions | umls-concept:C0034790 | lld:lifeskim |
pubmed-article:7680688 | lifeskim:mentions | umls-concept:C0024518 | lld:lifeskim |
pubmed-article:7680688 | lifeskim:mentions | umls-concept:C0021024 | lld:lifeskim |
pubmed-article:7680688 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:7680688 | lifeskim:mentions | umls-concept:C0040549 | lld:lifeskim |
pubmed-article:7680688 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:7680688 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:7680688 | lifeskim:mentions | umls-concept:C1705822 | lld:lifeskim |
pubmed-article:7680688 | lifeskim:mentions | umls-concept:C0348011 | lld:lifeskim |
pubmed-article:7680688 | lifeskim:mentions | umls-concept:C0181687 | lld:lifeskim |
pubmed-article:7680688 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
pubmed-article:7680688 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:7680688 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:7680688 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:7680688 | pubmed:dateCreated | 1993-4-13 | lld:pubmed |
pubmed-article:7680688 | pubmed:abstractText | We have used multiple-amino acid replacement mutagenesis to examine the roles of the TCR homologues of Ig complementarity-determining regions (CDR) and framework sequences in Ag-MHC and Staphylococcus aureus enterotoxin reactivity. In the three cases examined, transplantation of Ig CDR3 homologues between I-Ek-restricted TCR that recognize distinct peptides did not result in transfer of peptide reactivity. Thus the structural context of the CDR3 loops, e.g., both neighboring CDR and the V beta structure, must play a crucial, albeit supporting, role in ligand recognition. The extreme lability of this context was also shown by the fact that transplantation of the CDR1, -2, and -3 loops from the beta chain of 5C.C7 onto a V beta 1 framework failed to transfer MHC-peptide specificity even when the TCR-alpha chains were identical. In contrast, superantigen reactivity was readily transferred in several cases, with CDR2 transplants conferring strong staphylococcal enterotoxin B and A reactivity and CDR1 transplants yielding weak reactivities. This suggests that bacterial (and perhaps other) superantigens bind to many of the same regions of the TCR V beta that are believed to interact with MHC molecules. These regions of V beta may be ideal targets for superantigen binding precisely because they interact with MHC molecules and thus may be relatively conserved. | lld:pubmed |
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pubmed-article:7680688 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7680688 | pubmed:language | eng | lld:pubmed |
pubmed-article:7680688 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7680688 | pubmed:citationSubset | AIM | lld:pubmed |
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pubmed-article:7680688 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7680688 | pubmed:month | Mar | lld:pubmed |
pubmed-article:7680688 | pubmed:issn | 0022-1767 | lld:pubmed |
pubmed-article:7680688 | pubmed:author | pubmed-author:SonodaTT | lld:pubmed |
pubmed-article:7680688 | pubmed:author | pubmed-author:DavisM MMM | lld:pubmed |
pubmed-article:7680688 | pubmed:author | pubmed-author:PORTEOUSDD | lld:pubmed |
pubmed-article:7680688 | pubmed:author | pubmed-author:JorgensenJ... | lld:pubmed |
pubmed-article:7680688 | pubmed:author | pubmed-author:RockE PEP | lld:pubmed |
pubmed-article:7680688 | pubmed:author | pubmed-author:PattenP APA | lld:pubmed |
pubmed-article:7680688 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7680688 | pubmed:day | 15 | lld:pubmed |
pubmed-article:7680688 | pubmed:volume | 150 | lld:pubmed |
pubmed-article:7680688 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7680688 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7680688 | pubmed:pagination | 2281-94 | lld:pubmed |
pubmed-article:7680688 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:7680688 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:7680688 | pubmed:articleTitle | Transfer of putative complementarity-determining region loops of T cell receptor V domains confers toxin reactivity but not peptide/MHC specificity. | lld:pubmed |
pubmed-article:7680688 | pubmed:affiliation | Department of Microbiology and Immunology, Stanford University, CA 94305. | lld:pubmed |
pubmed-article:7680688 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7680688 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:7680688 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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