pubmed-article:17643103 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17643103 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
pubmed-article:17643103 | lifeskim:mentions | umls-concept:C0439148 | lld:lifeskim |
pubmed-article:17643103 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:17643103 | lifeskim:mentions | umls-concept:C0449450 | lld:lifeskim |
pubmed-article:17643103 | pubmed:issue | 9 | lld:pubmed |
pubmed-article:17643103 | pubmed:dateCreated | 2007-8-22 | lld:pubmed |
pubmed-article:17643103 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17643103 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17643103 | pubmed:abstractText | Interleukin 15 (IL-15) and IL-2, which promote the survival of memory CD8(+) T cells and regulatory T cells, respectively, bind receptor complexes that share beta- and gamma-signaling subunits. Receptor specificity is provided by unique, nonsignaling alpha-subunits. Whereas IL-2 receptor-alpha (IL-2Ralpha) is expressed together in cis with the beta- and gamma-subunits on T cells and B cells, IL-15Ralpha is expressed in trans on antigen-presenting cells. Here we present a 1.85-A crystal structure of the human IL-15-IL-15Ralpha complex. The structure provides insight into the molecular basis of the specificity of cytokine recognition and emphasizes the importance of water in generating this very high-affinity complex. Despite very low IL-15-IL-2 sequence homology and distinct receptor architecture, the topologies of the IL-15-IL-15Ralpha and IL-2-IL-2Ralpha complexes are very similar. Our data raise the possibility that IL-2, like IL-15, might be capable of being presented in trans in the context of its unique receptor alpha-chain. | lld:pubmed |
pubmed-article:17643103 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17643103 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17643103 | pubmed:language | eng | lld:pubmed |
pubmed-article:17643103 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17643103 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17643103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17643103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17643103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17643103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17643103 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17643103 | pubmed:month | Sep | lld:pubmed |
pubmed-article:17643103 | pubmed:issn | 1529-2908 | lld:pubmed |
pubmed-article:17643103 | pubmed:author | pubmed-author:YamagataYurik... | lld:pubmed |
pubmed-article:17643103 | pubmed:author | pubmed-author:DavisSimon... | lld:pubmed |
pubmed-article:17643103 | pubmed:author | pubmed-author:ShutoTsuyoshi... | lld:pubmed |
pubmed-article:17643103 | pubmed:author | pubmed-author:KaiHirofumiH | lld:pubmed |
pubmed-article:17643103 | pubmed:author | pubmed-author:IkemizuShinji... | lld:pubmed |
pubmed-article:17643103 | pubmed:author | pubmed-author:NakamuraTeruy... | lld:pubmed |
pubmed-article:17643103 | pubmed:author | pubmed-author:TomaSachikoS | lld:pubmed |
pubmed-article:17643103 | pubmed:author | pubmed-author:ChirifuMamiM | lld:pubmed |
pubmed-article:17643103 | pubmed:author | pubmed-author:HayashiChihar... | lld:pubmed |
pubmed-article:17643103 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17643103 | pubmed:volume | 8 | lld:pubmed |
pubmed-article:17643103 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17643103 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17643103 | pubmed:pagination | 1001-7 | lld:pubmed |
pubmed-article:17643103 | pubmed:dateRevised | 2010-4-30 | lld:pubmed |
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pubmed-article:17643103 | pubmed:meshHeading | pubmed-meshheading:17643103... | lld:pubmed |
pubmed-article:17643103 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17643103 | pubmed:articleTitle | Crystal structure of the IL-15-IL-15Ralpha complex, a cytokine-receptor unit presented in trans. | lld:pubmed |
pubmed-article:17643103 | pubmed:affiliation | Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-honmachi, Kumamoto 862-0973, Japan. | lld:pubmed |
pubmed-article:17643103 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17643103 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17643103 | lld:pubmed |