Abstract:
: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 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 TRα.
journal_name
FEBS Open Biojournal_title
FEBS open bioauthors
Fernandez EJ,Gahlot V,Rodriguez C,Amburn Jdoi
10.1002/2211-5463.12229subject
Has Abstractpub_date
2017-05-15 00:00:00pages
854-864issue
6issn
2211-5463pii
FEB412229journal_volume
7pub_type
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