The quaternary architecture of RARβ-RXRα heterodimer facilitates domain-domain signal transmission.

ABSTRACT: Assessing the physical connections and allosteric communications in multi-domain nuclear receptor (NR) polypeptides has remained challenging, with few crystal structures available to show their overall structural organizations. Here we report the quaternary architecture of multi-domain retinoic acid receptor β-retinoic X receptor α (RARβ-RXRα) heterodimer bound to DNA, ligands and coactivator peptides, examined through crystallographic, hydrogen-deuterium exchange mass spectrometry, mutagenesis and functional studies. The RARβ ligand-binding domain (LBD) and DNA-binding domain (DBD) are physically connected to foster allosteric signal transmission between them. Direct comparisons among all the multi-domain NRs studied crystallographically to date show significant variations within their qu

SUBMITTER: Chandra V 

PROVIDER: S-EPMC5636793 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature