pubmed-article:7969188 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7969188 | lifeskim:mentions | umls-concept:C0001483 | lld:lifeskim |
pubmed-article:7969188 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:7969188 | lifeskim:mentions | umls-concept:C0017355 | lld:lifeskim |
pubmed-article:7969188 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
pubmed-article:7969188 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:7969188 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
pubmed-article:7969188 | pubmed:issue | 16 | lld:pubmed |
pubmed-article:7969188 | pubmed:dateCreated | 1994-12-19 | lld:pubmed |
pubmed-article:7969188 | pubmed:abstractText | The adenovirus early region 3 glycoprotein E3-19k binds to and inhibits expression of class I major histocompatibility complex (MHC)-encoded molecules, which may help infected cells evade immune recognition. The role of specific regions of the class I MHC molecule in the interaction with E3-19k was evaluated using a series of HLA-A2.1-, HLA-A2 variant-, and HLA-B7-expressing cell lines. The monoclonal antibody (mAb) W6/32, which recognizes a monomorphic epitope on class I MHC molecules, readily co-immunoprecipitated E3-19k with HLA-A2.1 and 14 different HLA-A2 variant molecules that differ from HLA-A2.1 by single amino acid substitutions. Thus, no single residue tested in the regions of the class I MHC molecule that bind peptide or the T-cell receptor controls the binding to E3-19k. Additional immunoprecipitations performed with mAbs directed against well-defined epitopes on the surface of HLA-A2.1 revealed a dichotomy in the ability of the mAbs to co-immunoprecipitate HLA-A2.1 and E3-19k. The mAbs LGIII-220 (directed against the C-terminal end of the alpha 1-helix), CR11-351 (directed against the N-terminal end of the alpha 2-helix), and PA2.1 (directed against the middle of the alpha 2-helix and an underlying beta-loop) readily co-precipitated HLA-A2.1 and E3-19k. In contrast, mAbs MA2.1 (directed against the N-terminal end of the alpha 1-helix and the C-terminal end of the alpha 2-helix) and HO-2 (directed against the N-terminal end of the alpha 1-helix) did not co-precipitate E3-19k with HLA-A2.1. Similarly, mAb MB40.2 (directed against residues 169-182 of HLA-B7) also did not co-precipitate E3-19k with HLA-B7. These studies lead to the conclusion that the N-terminal end of the alpha 1-helix and the C-terminal end of the alpha 2-helix play an important role in dictating the ability of the E3-19k protein to bind to the class I MHC molecule. | lld:pubmed |
pubmed-article:7969188 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7969188 | pubmed:language | eng | lld:pubmed |
pubmed-article:7969188 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7969188 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7969188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7969188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7969188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7969188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7969188 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7969188 | pubmed:month | Nov | lld:pubmed |
pubmed-article:7969188 | pubmed:issn | 0161-5890 | lld:pubmed |
pubmed-article:7969188 | pubmed:author | pubmed-author:GutierrezEE | lld:pubmed |
pubmed-article:7969188 | pubmed:author | pubmed-author:FlomenbergPP | lld:pubmed |
pubmed-article:7969188 | pubmed:author | pubmed-author:HoganK TKT | lld:pubmed |
pubmed-article:7969188 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7969188 | pubmed:volume | 31 | lld:pubmed |
pubmed-article:7969188 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7969188 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7969188 | pubmed:pagination | 1277-84 | lld:pubmed |
pubmed-article:7969188 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:7969188 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:7969188 | pubmed:articleTitle | Identification of class I MHC regions which bind to the adenovirus E3-19k protein. | lld:pubmed |
pubmed-article:7969188 | pubmed:affiliation | Department of Medicine, Medical College of Wisconsin, Milwaukee. | lld:pubmed |
pubmed-article:7969188 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7969188 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:7969188 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7969188 | lld:pubmed |