pubmed-article:10993729 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10993729 | lifeskim:mentions | umls-concept:C0521026 | lld:lifeskim |
pubmed-article:10993729 | lifeskim:mentions | umls-concept:C1335376 | lld:lifeskim |
pubmed-article:10993729 | lifeskim:mentions | umls-concept:C0034790 | lld:lifeskim |
pubmed-article:10993729 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:10993729 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
pubmed-article:10993729 | lifeskim:mentions | umls-concept:C0441889 | lld:lifeskim |
pubmed-article:10993729 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
pubmed-article:10993729 | lifeskim:mentions | umls-concept:C1518124 | lld:lifeskim |
pubmed-article:10993729 | lifeskim:mentions | umls-concept:C0392762 | lld:lifeskim |
pubmed-article:10993729 | lifeskim:mentions | umls-concept:C0870509 | lld:lifeskim |
pubmed-article:10993729 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:10993729 | pubmed:dateCreated | 2000-10-17 | lld:pubmed |
pubmed-article:10993729 | pubmed:abstractText | Viral escape, first characterized for the lymphocytic choriomeningitis virus (LCMV) in a mouse transgenic for the P14 T cell-receptor (TCR), can be due to mutations in T-cell epitopes. We have measured the affinity between the H-2D(b) containing the wild-type and two of its "viral escape" epitopes, as well as other altered peptide ligands (APL), by using BIACORE analysis, and solved the crystal structure of H-2D(b) in complex with the wild-type peptide at 2.75 A resolution. We show that viral escape is due to a 50 to 100-fold reduction in the level of affinity between the P14 TCR and the binary complexes of the MHC molecule with the different peptides. Structurally, one of the mutations alters a TCR contact residue, while the effect of the other on the binding of the TCR must be indirect through structural rearrangements. The former is a null ligand, while the latter still leads to some central tolerance. This work defines the structural and energetic threshold for viral escape. | lld:pubmed |
pubmed-article:10993729 | pubmed:language | eng | lld:pubmed |
pubmed-article:10993729 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10993729 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10993729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10993729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10993729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10993729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10993729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10993729 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10993729 | pubmed:month | Sep | lld:pubmed |
pubmed-article:10993729 | pubmed:issn | 0022-2836 | lld:pubmed |
pubmed-article:10993729 | pubmed:author | pubmed-author:GrütterM GMG | lld:pubmed |
pubmed-article:10993729 | pubmed:author | pubmed-author:PlückthunAA | lld:pubmed |
pubmed-article:10993729 | pubmed:author | pubmed-author:MiskaR MRM | lld:pubmed |
pubmed-article:10993729 | pubmed:author | pubmed-author:TissotA CAC | lld:pubmed |
pubmed-article:10993729 | pubmed:author | pubmed-author:CiattoCC | lld:pubmed |
pubmed-article:10993729 | pubmed:copyrightInfo | Copyright 2000 Academic Press. | lld:pubmed |
pubmed-article:10993729 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10993729 | pubmed:day | 29 | lld:pubmed |
pubmed-article:10993729 | pubmed:volume | 302 | lld:pubmed |
pubmed-article:10993729 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10993729 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10993729 | pubmed:pagination | 873-85 | lld:pubmed |
pubmed-article:10993729 | pubmed:dateRevised | 2004-2-12 | lld:pubmed |
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pubmed-article:10993729 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10993729 | pubmed:articleTitle | Viral escape at the molecular level explained by quantitative T-cell receptor/peptide/MHC interactions and the crystal structure of a peptide/MHC complex. | lld:pubmed |
pubmed-article:10993729 | pubmed:affiliation | Biochemisches Institut der Universität Zürich, Winterthurerstrasse 190, Zürich, CH-8057, Switzerland. | lld:pubmed |
pubmed-article:10993729 | pubmed:publicationType | Journal Article | lld:pubmed |
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