| pubmed-article:16041067 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16041067 | lifeskim:mentions | umls-concept:C1175175 | lld:lifeskim |
| pubmed-article:16041067 | lifeskim:mentions | umls-concept:C1333899 | lld:lifeskim |
| pubmed-article:16041067 | lifeskim:mentions | umls-concept:C0178774 | lld:lifeskim |
| pubmed-article:16041067 | lifeskim:mentions | umls-concept:C0019728 | lld:lifeskim |
| pubmed-article:16041067 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:16041067 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:16041067 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16041067 | pubmed:issue | Pt 8 | lld:pubmed |
| pubmed-article:16041067 | pubmed:dateCreated | 2005-7-25 | lld:pubmed |
| pubmed-article:16041067 | pubmed:abstractText | The structure of the human MHC-I molecule HLA-A*1101 in complex with a nonameric peptide (KTFPPTEPK) has been determined by X-ray crystallography to 1.45 A resolution. The peptide is derived from the SARS-CoV nucleocapsid protein positions 362-370 (SNP362-370). It is conserved in all known isolates of SARS-CoV and has been verified by in vitro peptide-binding studies to be a good to intermediate binder to HLA-A*0301 and HLA-A*1101, with IC50 values of 70 and 186 nM, respectively [Sylvester-Hvid et al. (2004), Tissue Antigens, 63, 395-400]. In terms of the residues lining the peptide-binding groove, the HLA-A*1101-SNP362-370 complex is very similar to other known structures of HLA-A*1101 and HLA-A*6801. The SNP362-370 peptide is held in place by 17 hydrogen bonds to the alpha-chain residues and by nine water molecules which are also tightly bound in the peptide-binding groove. Thr6 of the peptide (Thr6p) does not make efficient use of the middle (E) pocket. For vaccine development, there seems to be a potential for optimization targeted at this position. All residues except Thr2p and Lys9p are accessible for T-cell recognition. | lld:pubmed |
| pubmed-article:16041067 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16041067 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16041067 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16041067 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16041067 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16041067 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16041067 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16041067 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16041067 | pubmed:issn | 0907-4449 | lld:pubmed |
| pubmed-article:16041067 | pubmed:author | pubmed-author:GajhedeMichae... | lld:pubmed |
| pubmed-article:16041067 | pubmed:author | pubmed-author:BuusSørenS | lld:pubmed |
| pubmed-article:16041067 | pubmed:author | pubmed-author:BlicherThomas... | lld:pubmed |
| pubmed-article:16041067 | pubmed:author | pubmed-author:KastrupJette... | lld:pubmed |
| pubmed-article:16041067 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16041067 | pubmed:volume | 61 | lld:pubmed |
| pubmed-article:16041067 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16041067 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16041067 | pubmed:pagination | 1031-40 | lld:pubmed |
| pubmed-article:16041067 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:16041067 | pubmed:meshHeading | pubmed-meshheading:16041067... | lld:pubmed |
| pubmed-article:16041067 | pubmed:meshHeading | pubmed-meshheading:16041067... | lld:pubmed |
| pubmed-article:16041067 | pubmed:meshHeading | pubmed-meshheading:16041067... | lld:pubmed |
| pubmed-article:16041067 | pubmed:meshHeading | pubmed-meshheading:16041067... | lld:pubmed |
| pubmed-article:16041067 | pubmed:meshHeading | pubmed-meshheading:16041067... | lld:pubmed |
| pubmed-article:16041067 | pubmed:meshHeading | pubmed-meshheading:16041067... | lld:pubmed |
| pubmed-article:16041067 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16041067 | pubmed:articleTitle | High-resolution structure of HLA-A*1101 in complex with SARS nucleocapsid peptide. | lld:pubmed |
| pubmed-article:16041067 | pubmed:affiliation | Biostructural Research, Department of Medicinal Chemistry, The Danish University of Pharmaceutical Sciences, Universitetsparken 2, DK-2100 Copenhagen, Denmark. | lld:pubmed |
| pubmed-article:16041067 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16041067 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:16041067 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16041067 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:3105 | entrezgene:pubmed | pubmed-article:16041067 | lld:entrezgene |
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