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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2000-7-17
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pubmed:databankReference |
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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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Benzoates,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Retinoic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoid X Receptors,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoids,
http://linkedlifedata.com/resource/pubmed/chemical/SR 11237,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/retinoic acid receptor alpha
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
289-98
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10882070-Amino Acid Sequence,
pubmed-meshheading:10882070-Animals,
pubmed-meshheading:10882070-Benzoates,
pubmed-meshheading:10882070-Binding Sites,
pubmed-meshheading:10882070-Crystallography, X-Ray,
pubmed-meshheading:10882070-Dimerization,
pubmed-meshheading:10882070-Fatty Acids,
pubmed-meshheading:10882070-Humans,
pubmed-meshheading:10882070-Ligands,
pubmed-meshheading:10882070-Mice,
pubmed-meshheading:10882070-Models, Molecular,
pubmed-meshheading:10882070-Molecular Sequence Data,
pubmed-meshheading:10882070-Receptors, Retinoic Acid,
pubmed-meshheading:10882070-Recombinant Proteins,
pubmed-meshheading:10882070-Retinoid X Receptors,
pubmed-meshheading:10882070-Retinoids,
pubmed-meshheading:10882070-Signal Transduction,
pubmed-meshheading:10882070-Surface Properties,
pubmed-meshheading:10882070-Transcription Factors
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pubmed:year |
2000
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pubmed:articleTitle |
Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains.
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pubmed:affiliation |
Institut de Génétique et de Biologie Moléculaire et Cellulaire, CRNS/INSERM/Université Louis Pasteur/Collège de France, Illkirch, Strasbourg.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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