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Updated: Sep 30, 2026

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists
Published on: November 15, 2013
Ligand and coactivator recruitment preferences of peroxisome proliferator activated receptor alpha
Ranjan Mukherjee1, Shaoxian Sun, Linda Santomenna
1Cardiovascular Diseases Research, Bristol-Myers Squibb Company, Experimental Station, E400 Wilmington, DE 19880, USA. ranjan.mukherjee@bms.com
Abstract:
The mechanism by which ligands of nuclear receptors show differential effects on gene transcription is not fully understood, but is believed to result in part from the preferential recruitment and/or displacement of coactivators and corepressors. We have explored the interaction of several known ligands and the nuclear receptor (peroxisome proliferator activated receptor alpha, PPARalpha) using scintillation proximity assay (SPA) and the interaction of LXXLL containing peptides derived from three coactivators (SRC-1, CBP and PGC-1) with PPARalpha in the presence of PPARalpha agonist ligands using fluorescence resonance energy transfer (FRET). The EC(50)s of the individual ligands for recruitment showed the same rank order regardless of the coactivator peptide used, with GW2331
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