Molecular determinants of MED1 interaction with the DNA bound VDR-RXR heterodimer.

ABSTRACT: The MED1 subunit of the Mediator complex is an essential coactivator of nuclear receptor-mediated transcriptional activation. While structural requirements for ligand-dependent binding of classical coactivator motifs of MED1 to numerous nuclear receptor ligand-binding domains have been fully elucidated, the recognition of the full-length or truncated coactivator by full nuclear receptor complexes remain unknown. Here we present structural details of the interaction between a large part of MED1 comprising its structured N-terminal and the flexible receptor-interacting domains and the mutual heterodimer of the vitamin D receptor (VDR) and the retinoid X receptor (RXR) bound to their cognate DNA response element. Using a combination of structural and biophysical methods we show that the ligan

SUBMITTER: Belorusova AY 

PROVIDER: S-EPMC7641746 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature