Source Publication
FEBS Open Bio
Document Type
Article
Publication Date
6-5-2017
DOI
10.1002/2211-5463.12229
Abstract
The A/B domains of nuclear receptors such as thyroid receptor a (TRa) 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 distinct molecular factors of the transcriptional preinitiation complex. We further suggest that by influencing the affinity of the DBD for DNA, A/B domain can fine-tune the recognition of promotor DNA by TRa.
Recommended Citation
Fernandez, Elias J., Vandna Gahlot, Celeste Rodriguez, and Jacob Amburn, “DNA-Induced Unfolding of the Thyroid Hormone Receptor α A/B Domain through Allostery,” FEBS Open Bio 7, no. 6 (2017), 854-864. doi: 10.1002/2211-5463.12229
Submission Type
Publisher's Version
Comments
This article was published openly thanks to the University of Tennessee Open Publishing Support Fund.
Licensed under a Creative Commons Attribution 4.0 International license.