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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2003-5-16
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pubmed:abstractText |
Based on the folding conservation across the nuclear receptor superfamily and the sequence homology with RAR-gamma, we report the construction of a three dimensional model of the ligand binding domain of FXR. The model is exploited for the elucidation of the binding mode of 6alpha-ethyl-chenodeoxycholic acid. The results of the docking experiments give quite clear indications that the bile acid derivative would bind the receptor in a mode significantly different than that observed for agonists of other 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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0960-894X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1865-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12749886-Amino Acid Sequence,
pubmed-meshheading:12749886-Bile Acids and Salts,
pubmed-meshheading:12749886-Binding Sites,
pubmed-meshheading:12749886-Chenodeoxycholic Acid,
pubmed-meshheading:12749886-DNA-Binding Proteins,
pubmed-meshheading:12749886-Humans,
pubmed-meshheading:12749886-Models, Molecular,
pubmed-meshheading:12749886-Molecular Sequence Data,
pubmed-meshheading:12749886-Protein Binding,
pubmed-meshheading:12749886-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:12749886-Receptors, Retinoic Acid,
pubmed-meshheading:12749886-Sequence Alignment,
pubmed-meshheading:12749886-Sequence Homology, Amino Acid,
pubmed-meshheading:12749886-Transcription Factors
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pubmed:year |
2003
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pubmed:articleTitle |
Binding mode of 6ECDCA, a potent bile acid agonist of the farnesoid X receptor (FXR).
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pubmed:affiliation |
Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, Via del Liceo 1, 06123 Perugia, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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