Linked Life Data

14622968

Source:http://linkedlifedata.com/resource/pubmed/id/14622968

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pubmed-article:14622968pubmed:abstractTextThe ligand-binding domain (LBD) of the human retinoic acid receptor-related orphan receptor (RORalpha-LBD), expressed in Sf9 cells, was purified and analyzed by electrospray ionization-mass spectrometry (ESI-MS). ESI-MS operated under native conditions showed the presence of a fortuitous ligand with molecular weight 386. Further analysis by gas chromatography-mass spectrometry (GC-MS) allowed the identification of the ligands bound to the LBD. Cholesterol (77%) and 7-dehydrocholesterol (provitamin D(3); 18%) were shown to be the major ligands. A monohydroxylated cholesterol derivative was identified as a minor ligand. In addition, ligand exchange experiments monitored by ESI-MS showed that cholesterol sulfate has a higher affinity for RORalpha-LBD than cholesterol and 25-hydroxycholesterol. Binding of coactivator (CoA) peptide GRIP1P was shown to occur in a stoichiometric manner. Therefore, monitoring of binding of CoAs by mass spectrometry could be used for classification of the ligands as agonist or antagonist molecules.lld:pubmed
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pubmed-article:14622968pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:14622968pubmed:articleTitleIdentification of natural ligands of retinoic acid receptor-related orphan receptor alpha ligand-binding domain expressed in Sf9 cells--a mass spectrometry approach.lld:pubmed
pubmed-article:14622968pubmed:affiliationCentral Technologies, Novartis Institutes for Biomedical Research, Lichtstrasse 35, CH-4002 Basel, Switzerland. francis.bitsch@pharma.novartis.comlld:pubmed
pubmed-article:14622968pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:14622968pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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