Nuclear Receptor Interdomain Communication is Mediated by the Hinge with Ligand Specificity
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Abstract
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These results suggest an important role for the hinge in mediating contact between LBD and DBD, as well as the ligand-specific nature of this interaction.
This is a really interesting study on the complex interplay between NHR domains! I was wondering if you tested interactions between these domains using in vitro protein-protein interaction assays that can sidestep possible complications of the heterologous cell-based Gal4 system (i.e. “pull-down” assays, etc.)?
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As nuclear receptors share a conserved structure and mechanism, we anticipate that similar ligand-modulated domain rearrangement will be observed in other receptors
Are there any naturally occurring mutations associated with diseases that map to regions that your model predicts would disrupt interdomain interactions? Or conversely, can you generate mutations that your model predicts would disrupt interactions and measure the effects on transcription use simple reporter assays and full-length constructs?
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