Ontology highlight
ABSTRACT:
SUBMITTER: Fernandez EJ
PROVIDER: S-EPMC5458466 | biostudies-other | 2017 Jun
REPOSITORIES: biostudies-other
Fernandez Elias J EJ Gahlot Vandna V Rodriguez Celeste C Amburn Jacob J
FEBS open bio 20170515 6
The A/B domains of nuclear receptors such as thyroid receptor α (TRα) are considered to be conformationally flexible and can potentially adopt multiple structural conformations. We used intrinsic tryptophan fluorescence quenching and circular dichroism spectroscopy to characterize the unfolding of this A/B domain upon DNA binding to the contiguous DNA-binding domain (DBD). We propose that this allosteric change in A/B domain conformation can allow it to make the multiple interactions with distin ...[more]