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| pubmed-article:10882070 | lifeskim:mentions | umls-concept:C1366536 | lld:lifeskim |
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| pubmed-article:10882070 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:10882070 | lifeskim:mentions | umls-concept:C1148772 | lld:lifeskim |
| pubmed-article:10882070 | lifeskim:mentions | umls-concept:C1549879 | lld:lifeskim |
| pubmed-article:10882070 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10882070 | pubmed:dateCreated | 2000-7-17 | lld:pubmed |
| pubmed-article:10882070 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10882070 | pubmed:abstractText | The crystal structure of a heterodimer between the ligand-binding domains (LBDs) of the human RARalpha bound to a selective antagonist and the constitutively active mouse RXRalphaF318A mutant shows that, pushed by a bulky extension of the ligand, RARalpha helix H12 adopts an antagonist position. The unexpected presence of a fatty acid in the ligand-binding pocket of RXRalpha(F318A is likely to account for its apparent "constitutivity." Specific conformational changes suggest the structural basis of pure and partial antagonism. The RAR-RXR heterodimer interface is similar to that observed in most nuclear receptor (NR) homodimers. A correlative analysis of 3D structures and sequences provides a novel view on dimerization among members of the nuclear receptor superfamily. | lld:pubmed |
| pubmed-article:10882070 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10882070 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10882070 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10882070 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10882070 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:10882070 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:10882070 | pubmed:author | pubmed-author:ChambonPP | lld:pubmed |
| pubmed-article:10882070 | pubmed:author | pubmed-author:MorayNN | lld:pubmed |
| pubmed-article:10882070 | pubmed:author | pubmed-author:VivatVV | lld:pubmed |
| pubmed-article:10882070 | pubmed:author | pubmed-author:BourguetWW | lld:pubmed |
| pubmed-article:10882070 | pubmed:author | pubmed-author:GronemeyerHH | lld:pubmed |
| pubmed-article:10882070 | pubmed:author | pubmed-author:WurtzJ MJM | lld:pubmed |
| pubmed-article:10882070 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10882070 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:10882070 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10882070 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10882070 | pubmed:pagination | 289-98 | lld:pubmed |
| pubmed-article:10882070 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10882070 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10882070 | pubmed:articleTitle | Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. | lld:pubmed |
| pubmed-article:10882070 | pubmed:affiliation | Institut de Génétique et de Biologie Moléculaire et Cellulaire, CRNS/INSERM/Université Louis Pasteur/Collège de France, Illkirch, Strasbourg. | lld:pubmed |
| pubmed-article:10882070 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10882070 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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