Phosphorylation-Regulated Conformational Diversity and Topological Dynamics of an Intrinsically Disordered Nuclear Receptor
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The ability of AF1c phosphovariants to adopt multiple structural changes likely creates distinct binding surfaces within the NTD, enabling GR to selectively interact with different regulatory complexes along its signal transduction pathway.
This is a very insightful study! I'm curious if you can model how this newly formed helical structure binds to AF1 interacting domains present on such proteins as TBP?
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Importantly, reversible protein phosphorylation provides a major regulatory mechanism in conformational dynamics and compaction of IDPs
Have you explored whether this phosphorylation-dependent structural rearrangement may play a role in the function of other NHR AF1 or F domains?
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