Title : Phosphorylation of an intrinsically disordered segment in Ets1 shifts conformational sampling toward binding-competent substates.

Pub. Date : 2014 Aug 5

PMID : 25017730






1 Functional Relationships(s)
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1 By combining molecular dynamics simulations and protein docking, we demonstrate that the addition of phosphates to an ID segment adjacent to the PNT domain of Ets1 directs conformational sampling toward substates that are most compatible with high-affinity binding of the TAZ1 domain of its coactivator CBP. Phosphates zinc finger and BTB domain containing 18 Homo sapiens