Molecular Dynamics of "Fuzzy" Transcriptional Activator-Coactivator Interactions.

ABSTRACT: Transcriptional activation domains (ADs) are generally thought to be intrinsically unstructured, but capable of adopting limited secondary structure upon interaction with a coactivator surface. The indeterminate nature of this interface made it hitherto difficult to study structure/function relationships of such contacts. Here we used atomistic accelerated molecular dynamics (aMD) simulations to study the conformational changes of the GCN4 AD and variants thereof, either free in solution, or bound to the GAL11 coactivator surface. We show that the AD-coactivator interactions are highly dynamic while obeying distinct rules. The data provide insights into the constant and variable aspects of orientation of ADs relative to the coactivator, changes in secondary structure and energetic contribu

SUBMITTER: Scholes NS 

PROVIDER: S-EPMC4866707 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature