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Conformational selection: Vs. induced fit: Insights into the binding mechanisms of p38α MAP Kinase inhibitors

Chemical Communications, ISSN: 1364-548X, Vol: 56, Issue: 62, Page: 8818-8821
2020
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Article Description

The conformational dynamics of a kinase's activation loop have been challenging to assess due to the activation loop's intrinsic flexibility. To directly probe the conformational equilibrium of the activation loop of mitogen-activated protein kinase p38α, we present an approach based on site-directed spin labeling, electron paramagnetic resonance (EPR) distance restraints, and multilateration. We demonstrate that the activation loop of apo p38α resides in a highly flexible equilibrium state and we reveal that binding of small molecules significantly alters this equilibrium and the populated sub-states. This journal is

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