Defining the communication between agonist and coactivator binding in the retinoid X receptor α ligand binding domain.

ABSTRACT: Retinoid X receptors (RXRs) are obligate partners for several other nuclear receptors, and they play a key role in several signaling processes. Despite being a promiscuous heterodimer partner, this nuclear receptor is a target of therapeutic intervention through activation using selective RXR agonists (rexinoids). Agonist binding to RXR initiates a large conformational change in the receptor that allows for coactivator recruitment to its surface and enhanced transcription. Here we reveal the structural and dynamical changes produced when a coactivator peptide binds to the human RXRα ligand binding domain containing two clinically relevant rexinoids, Targretin and 9-cis-UAB30. Our results show that the structural changes are very similar for each rexinoid and similar to those for the pan-ag

SUBMITTER: Boerma LJ 

PROVIDER: S-EPMC3887207 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature