Nuclear hormone receptors coordinately regulate the activity of genetic networks through the
recruitment of transcriptional co-regulators, including co-repressors and co-activators.
Allosteric modulation of the ligand-binding domain by hormonal activators shifts the co-factor
binding preference by defined structural changes in overlapping docking sites. We report
here that mutations at conserved residues within the docking motif of the retinoic acid
receptor α cause defects in dimerization, co-regulator association, and transcriptional …