| pubmed-article:17082606 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17082606 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
| pubmed-article:17082606 | lifeskim:mentions | umls-concept:C0003320 | lld:lifeskim |
| pubmed-article:17082606 | lifeskim:mentions | umls-concept:C0034790 | lld:lifeskim |
| pubmed-article:17082606 | lifeskim:mentions | umls-concept:C0678836 | lld:lifeskim |
| pubmed-article:17082606 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:17082606 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:17082606 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:17082606 | pubmed:dateCreated | 2006-11-3 | lld:pubmed |
| pubmed-article:17082606 | pubmed:abstractText | TCRs exhibit a high degree of Ag specificity, even though their affinity for the peptide/MHC ligand is in the micromolar range. To explore how Ag specificity is achieved, we studied murine T cells expressing high-affinity TCRs engineered by in vitro evolution for binding to hemoglobin peptide/class II complex (Hb/I-Ek). These TCRs were shown previously to maintain Ag specificity, despite having up to 800-fold higher affinity. We compared the response of the high-affinity TCRs and the low-affinity 3.L2 TCR toward a comprehensive set of peptides containing single substitutions at each TCR contact residue. This specificity analysis revealed that the increase in affinity resulted in a dramatic increase in the number of stimulatory peptides. The apparent discrepancy between observed degeneracy in the recognition of single amino acid-substituted Hb peptides and overall Ag specificity of the high-affinity TCRs was examined by generating chimeric peptides between the stimulatory Hb and nonstimulatory moth cytochrome c peptides. These experiments showed that MHC anchor residues significantly affected TCR recognition of peptide. The high-affinity TCRs allowed us to estimate the affinity, in the millimolar range, of immunologically relevant interactions of the TCR with peptide/MHC ligands that were previously unmeasurable because of their weak nature. Thus, through the study of high-affinity TCRs, we demonstrated that a TCR is more tolerant of single TCR contact residue substitutions than other peptide changes, revealing that recognition of Ag by T cells can exhibit both specificity and degeneracy. | lld:pubmed |
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| pubmed-article:17082606 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17082606 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17082606 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:17082606 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17082606 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:17082606 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:17082606 | pubmed:author | pubmed-author:AllenPaul MPM | lld:pubmed |
| pubmed-article:17082606 | pubmed:author | pubmed-author:WeberK... | lld:pubmed |
| pubmed-article:17082606 | pubmed:author | pubmed-author:KranzDavid... | lld:pubmed |
| pubmed-article:17082606 | pubmed:author | pubmed-author:DonermeyerDav... | lld:pubmed |
| pubmed-article:17082606 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17082606 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:17082606 | pubmed:volume | 177 | lld:pubmed |
| pubmed-article:17082606 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17082606 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17082606 | pubmed:pagination | 6911-9 | lld:pubmed |
| pubmed-article:17082606 | pubmed:dateRevised | 2007-12-3 | lld:pubmed |
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| pubmed-article:17082606 | pubmed:meshHeading | pubmed-meshheading:17082606... | lld:pubmed |
| pubmed-article:17082606 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:17082606 | pubmed:articleTitle | The study of high-affinity TCRs reveals duality in T cell recognition of antigen: specificity and degeneracy. | lld:pubmed |
| pubmed-article:17082606 | pubmed:affiliation | Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA. | lld:pubmed |
| pubmed-article:17082606 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17082606 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:17082606 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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