The Promiscuity of Allosteric Regulation of Nuclear Receptors by Retinoid X Receptor.

ABSTRACT: The promiscuous protein retinoid X receptor (RXR) displays essential allosteric regulation of several members in the nuclear hormone receptor superfamily via heterodimerization and (anti)cooperative binding of cognate ligands. Here, the structural basis of the positive allostery of RXR and constitutive androstane receptor (CAR) is revealed. In contrast, a similar computational approach had previously revealed the mechanism for negative allostery in the complex of RXR and thyroid receptor (TR). By comparing the positive and negative allostery of RXR complexed with CAR and TR respectively, we reported the promiscuous allosteric control involving RXR. We characterize the allosteric mechanism by expressing the correlated dynamics of selected residue-residue contacts which was extracted from at

SUBMITTER: Clark AK 

PROVIDER: S-EPMC5001894 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature