| pubmed-article:9110930 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9110930 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
| pubmed-article:9110930 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:9110930 | lifeskim:mentions | umls-concept:C0525038 | lld:lifeskim |
| pubmed-article:9110930 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:9110930 | lifeskim:mentions | umls-concept:C0062837 | lld:lifeskim |
| pubmed-article:9110930 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:9110930 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9110930 | pubmed:dateCreated | 1996-4-3 | lld:pubmed |
| pubmed-article:9110930 | pubmed:abstractText | The interaction between 9-mer peptides and HLA-B51 molecules was investigated by quantitative peptide binding assay using RMA-S cells expressing human beta2-microglobulin and HLA-B51 molecules. Of 147 chemically synthesized 9-mer peptides possessing two anchor residues corresponding to the motif of HLA-B*5101 binding self-peptides, 27 peptides bound to HLA-B*5101 molecules. Pro and Ala at position 2 as well as Ile at position 9 were confirmed to be main anchor residues, while Gly at position 2 as well as Val, Leu, and Met at position 9 were weak anchor residues for HLA-B*5101. The A-pocket is suspected to have a critical role in peptide binding to MHC class I molecules because this pocket corresponds to the N-terminus of peptides and has a strong hydrogen bond formed by conserved Tyr residues. Further analysis of peptide binding to HLA-B*5102 and B*5103 molecules showed that a single amino acid substitution of Tyr for His at residue 171(B*5102) and that of Gly for Trp at residue 167 (B*5103) has a minimum effect in HLA-B51-peptide binding. Since previous studies showed that some HLA-B51 alloreactive CTL clones failed to kill the cells expressing HLA-B*5102 or HLA-B*5103, these results imply that the structural change of the A-pocket among HLA-B51 subtypes causes a critical conformational change of the epitope for TCR recognition rather than influences the interaction between peptides and MHC class I molecules. | lld:pubmed |
| pubmed-article:9110930 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9110930 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9110930 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9110930 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9110930 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9110930 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9110930 | pubmed:issn | 0093-7711 | lld:pubmed |
| pubmed-article:9110930 | pubmed:author | pubmed-author:MiwaKK | lld:pubmed |
| pubmed-article:9110930 | pubmed:author | pubmed-author:KanekoYY | lld:pubmed |
| pubmed-article:9110930 | pubmed:author | pubmed-author:KikuchiAA | lld:pubmed |
| pubmed-article:9110930 | pubmed:author | pubmed-author:SakaguchiTT | lld:pubmed |
| pubmed-article:9110930 | pubmed:author | pubmed-author:TakiguchiMM | lld:pubmed |
| pubmed-article:9110930 | pubmed:author | pubmed-author:RammenseeH... | lld:pubmed |
| pubmed-article:9110930 | pubmed:author | pubmed-author:TakamiyaYY | lld:pubmed |
| pubmed-article:9110930 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9110930 | pubmed:volume | 43 | lld:pubmed |
| pubmed-article:9110930 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9110930 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9110930 | pubmed:pagination | 268-76 | lld:pubmed |
| pubmed-article:9110930 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:9110930 | pubmed:meshHeading | pubmed-meshheading:9110930-... | lld:pubmed |
| pubmed-article:9110930 | pubmed:meshHeading | pubmed-meshheading:9110930-... | lld:pubmed |
| pubmed-article:9110930 | pubmed:meshHeading | pubmed-meshheading:9110930-... | lld:pubmed |
| pubmed-article:9110930 | pubmed:meshHeading | pubmed-meshheading:9110930-... | lld:pubmed |
| pubmed-article:9110930 | pubmed:meshHeading | pubmed-meshheading:9110930-... | lld:pubmed |
| pubmed-article:9110930 | pubmed:meshHeading | pubmed-meshheading:9110930-... | lld:pubmed |
| pubmed-article:9110930 | pubmed:meshHeading | pubmed-meshheading:9110930-... | lld:pubmed |
| pubmed-article:9110930 | pubmed:meshHeading | pubmed-meshheading:9110930-... | lld:pubmed |
| pubmed-article:9110930 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:9110930 | pubmed:articleTitle | Binding of nonamer peptides to three HLA-B51 molecules which differ by a single amino acid substitution in the A-pocket. | lld:pubmed |
| pubmed-article:9110930 | pubmed:affiliation | Department of Tumor Biology, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minota-ku, Tokyo 108, Japan. | lld:pubmed |
| pubmed-article:9110930 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9110930 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9110930 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9110930 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9110930 | lld:pubmed |
