Patrick Roser, Jörn Weisner, Jeffrey R. Simard, Daniel Rauh and Malte Drescher
Chem. Commun., 2018,54, 12057-12060
DOI:
10.1039/C8CC06128A,
Communication
Conformational transitions in protein kinases are crucial for the biological function of these enzymes. Here, we characterize and assess conformational equilibria of the activation loop and the effect of small molecule inhibitors in the MAP kinase p38α. Our work experimentally revealed the existence of a two-state equilibrium for p38α while the addition of inhibitors shifts the equilibrium between these two states.
