| pubmed-article:15287746 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15287746 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
| pubmed-article:15287746 | lifeskim:mentions | umls-concept:C0019630 | lld:lifeskim |
| pubmed-article:15287746 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:15287746 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:15287746 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:15287746 | lifeskim:mentions | umls-concept:C2825311 | lld:lifeskim |
| pubmed-article:15287746 | lifeskim:mentions | umls-concept:C2349209 | lld:lifeskim |
| pubmed-article:15287746 | pubmed:issue | 31 | lld:pubmed |
| pubmed-article:15287746 | pubmed:dateCreated | 2004-8-3 | lld:pubmed |
| pubmed-article:15287746 | pubmed:abstractText | We used differential scanning calorimetry to study the thermal denaturation of murine major histocompatibility complex class II, I-E(k), accommodating hemoglobin (Hb) peptide mutants possessing a single amino acid substitution of the chemically conserved amino acids buried in the I-Ek pocket (positions 71 and 73) and exposed to the solvent (position 72). All of the I-Ek-Hb(mut) molecules exhibited greater thermal stability at pH 5.5 than at pH 7.4, as for the I-Ek-Hb(wt) molecule, which can explain the peptide exchange function of MHC II. The thermal stability was strongly dependent on the bound peptide sequences; the I-Ek-Hb(mut) molecules were less stable than the I-Ek-Hb(wt) molecules, in good correlation with the relative affinity of each peptide for I-Ek. This supports the notion that the bound peptide is part of the completely folded MHC II molecule. The thermodynamic parameters for I-Ek-Hb(mut) folding can explain the thermodynamic origin of the stability difference, in correlation with the crystal structural analysis, and the limited contributions of the residues to the overall conformation of the I-Ek-peptide complex. We found a linear relationship between the denaturation temperature and the calorimetric enthalpy change. Thus, although the MHC II-peptide complex could have a diverse thermal stability spectrum, depending on the amino acid sequences of the bound peptides, the conformational perturbations are limited. The variations in the MHC II-peptide complex stability would function in antigen recognition by the T cell receptor by affecting the stability of the MHC II-peptide-T cell receptor ternary complex. | lld:pubmed |
| pubmed-article:15287746 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15287746 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15287746 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15287746 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15287746 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15287746 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15287746 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15287746 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15287746 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15287746 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15287746 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:15287746 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:15287746 | pubmed:author | pubmed-author:SaraiAkinoriA | lld:pubmed |
| pubmed-article:15287746 | pubmed:author | pubmed-author:OdaMasayukiM | lld:pubmed |
| pubmed-article:15287746 | pubmed:author | pubmed-author:AzumaTakachik... | lld:pubmed |
| pubmed-article:15287746 | pubmed:author | pubmed-author:KozonoHaruoH | lld:pubmed |
| pubmed-article:15287746 | pubmed:author | pubmed-author:SaitoKeigoK | lld:pubmed |
| pubmed-article:15287746 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15287746 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:15287746 | pubmed:volume | 43 | lld:pubmed |
| pubmed-article:15287746 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15287746 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15287746 | pubmed:pagination | 10186-91 | lld:pubmed |
| pubmed-article:15287746 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15287746 | pubmed:meshHeading | pubmed-meshheading:15287746... | lld:pubmed |
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| pubmed-article:15287746 | pubmed:meshHeading | pubmed-meshheading:15287746... | lld:pubmed |
| pubmed-article:15287746 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15287746 | pubmed:articleTitle | Bound peptide-dependent thermal stability of major histocompatibility complex class II molecule I-Ek. | lld:pubmed |
| pubmed-article:15287746 | pubmed:affiliation | Research Institute for Biological Sciences, Tokyo University of Science, 2669, Yamazaki, Noda, Chiba 278-0022, Japan. | lld:pubmed |
| pubmed-article:15287746 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15287746 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
