Abstract:Auto-phosphorylation controls the transition between discrete functional and conformational states in protein kinases, yet the structural and molecular determinants underlaying this fundamental process remain unclear. Here we show that c-terminal Tyr 530 is a de facto c-Src auto-phosphorylation site with slow time-resolution kinetics and strong intermolecular component. On the contrary, activation-loop Tyr 419 undergoes fast kinetics and a cis-to-trans phosphorylation-switch that controls c-terminal Tyr 530 au… Show more
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