| pubmed-article:15020763 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15020763 | lifeskim:mentions | umls-concept:C2362561 | lld:lifeskim |
| pubmed-article:15020763 | lifeskim:mentions | umls-concept:C0007570 | lld:lifeskim |
| pubmed-article:15020763 | lifeskim:mentions | umls-concept:C0003316 | lld:lifeskim |
| pubmed-article:15020763 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:15020763 | lifeskim:mentions | umls-concept:C0449450 | lld:lifeskim |
| pubmed-article:15020763 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:15020763 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:15020763 | pubmed:dateCreated | 2004-3-25 | lld:pubmed |
| pubmed-article:15020763 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15020763 | pubmed:abstractText | Celiac disease, also known as celiac sprue, is a gluten-induced autoimmune-like disorder of the small intestine, which is strongly associated with HLA-DQ2. The structure of DQ2 complexed with an immunogenic epitope from gluten, QLQPFPQPELPY, has been determined to 2.2-A resolution by x-ray crystallography. The glutamate at P6, which is formed by tissue transglutaminase-catalyzed deamidation, is an important anchor residue as it participates in an extensive hydrogen-bonding network involving Lys-beta71 of DQ2. The gluten peptide-DQ2 complex retains critical hydrogen bonds between the MHC and the peptide backbone despite the presence of many proline residues in the peptide that are unable to participate in amide-mediated hydrogen bonds. Positioning of proline residues such that they do not interfere with backbone hydrogen bonding results in a reduction in the number of registers available for gluten peptides to bind to MHC class II molecules and presumably impairs the likelihood of establishing favorable side-chain interactions. The HLA association in celiac disease can be explained by a superior ability of DQ2 to bind the biased repertoire of proline-rich gluten peptides that have survived gastrointestinal digestion and that have been deamidated by tissue transglutaminase. Finally, surface-exposed proline residues in the proteolytically resistant ligand were replaced with functionalized analogs, thereby providing a starting point for the design of orally active agents for blocking gluten-induced toxicity. | lld:pubmed |
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| pubmed-article:15020763 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15020763 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15020763 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15020763 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15020763 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:15020763 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:15020763 | pubmed:author | pubmed-author:KhoslaChaitan... | lld:pubmed |
| pubmed-article:15020763 | pubmed:author | pubmed-author:KimChu-YoungC... | lld:pubmed |
| pubmed-article:15020763 | pubmed:author | pubmed-author:SollidLudvig... | lld:pubmed |
| pubmed-article:15020763 | pubmed:author | pubmed-author:QuarstenHanne... | lld:pubmed |
| pubmed-article:15020763 | pubmed:author | pubmed-author:BergsengElinE | lld:pubmed |
| pubmed-article:15020763 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15020763 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:15020763 | pubmed:volume | 101 | lld:pubmed |
| pubmed-article:15020763 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15020763 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15020763 | pubmed:pagination | 4175-9 | lld:pubmed |
| pubmed-article:15020763 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:15020763 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15020763 | pubmed:articleTitle | Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac disease. | lld:pubmed |
| pubmed-article:15020763 | pubmed:affiliation | Department of Chemical Engineering, Stanford University, Stanford, CA 94305, USA. | lld:pubmed |
| pubmed-article:15020763 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15020763 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15020763 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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