pubmed-article:16314439 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16314439 | lifeskim:mentions | umls-concept:C0026969 | lld:lifeskim |
pubmed-article:16314439 | lifeskim:mentions | umls-concept:C0038727 | lld:lifeskim |
pubmed-article:16314439 | lifeskim:mentions | umls-concept:C0004368 | lld:lifeskim |
pubmed-article:16314439 | lifeskim:mentions | umls-concept:C1413210 | lld:lifeskim |
pubmed-article:16314439 | lifeskim:mentions | umls-concept:C1441547 | lld:lifeskim |
pubmed-article:16314439 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:16314439 | lifeskim:mentions | umls-concept:C0449450 | lld:lifeskim |
pubmed-article:16314439 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
pubmed-article:16314439 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:16314439 | pubmed:dateCreated | 2005-12-6 | lld:pubmed |
pubmed-article:16314439 | pubmed:abstractText | Sulfatide derived from the myelin stimulates a distinct population of CD1d-restricted natural killer T (NKT) cells. Cis-tetracosenoyl sulfatide is one of the immunodominant species in myelin as identified by proliferation, cytokine secretion, and CD1d tetramer staining. The crystal structure of mouse CD1d in complex with cis-tetracosenoyl sulfatide at 1.9 A resolution reveals that the longer cis-tetracosenoyl fatty acid chain fully occupies the A' pocket of the CD1d binding groove, whereas the sphingosine chain fills up the F' pocket. A precise hydrogen bond network in the center of the binding groove orients and positions the ceramide backbone for insertion of the lipid tails in their respective pockets. The 3'-sulfated galactose headgroup is highly exposed for presentation to the T cell receptor and projects up and away from the binding pocket due to its beta linkage, compared with the more intimate binding of the alpha-glactosyl ceramide headgroup to CD1d. These structure and binding data on sulfatide presentation by CD1d have important implications for the design of therapeutics that target T cells reactive for myelin glycolipids in autoimmune diseases of the central nervous system. | lld:pubmed |
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pubmed-article:16314439 | pubmed:language | eng | lld:pubmed |
pubmed-article:16314439 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16314439 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16314439 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:16314439 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16314439 | pubmed:month | Dec | lld:pubmed |
pubmed-article:16314439 | pubmed:issn | 0022-1007 | lld:pubmed |
pubmed-article:16314439 | pubmed:author | pubmed-author:WilsonIan AIA | lld:pubmed |
pubmed-article:16314439 | pubmed:author | pubmed-author:WongChi-HueyC... | lld:pubmed |
pubmed-article:16314439 | pubmed:author | pubmed-author:RoyKeshabK | lld:pubmed |
pubmed-article:16314439 | pubmed:author | pubmed-author:KumarVipinV | lld:pubmed |
pubmed-article:16314439 | pubmed:author | pubmed-author:MaricicIgorI | lld:pubmed |
pubmed-article:16314439 | pubmed:author | pubmed-author:ZajoncDirk... | lld:pubmed |
pubmed-article:16314439 | pubmed:author | pubmed-author:WuDouglassD | lld:pubmed |
pubmed-article:16314439 | pubmed:author | pubmed-author:HalderRameshR | lld:pubmed |
pubmed-article:16314439 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16314439 | pubmed:day | 5 | lld:pubmed |
pubmed-article:16314439 | pubmed:volume | 202 | lld:pubmed |
pubmed-article:16314439 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16314439 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16314439 | pubmed:pagination | 1517-26 | lld:pubmed |
pubmed-article:16314439 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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