Publikation: Conformational selection vs. induced fit : insights into the binding mechanisms of p38α MAP Kinase inhibitors
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Chemical Communications. Royal Society of Chemistry (RSC). 2020, 56(62), pp. 8818-8821. ISSN 1359-7345. eISSN 1364-548X. Available under: doi: 10.1039/d0cc02539a
Zusammenfassung
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.
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540 Chemie
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ROSER, Patrick, Jörn WEISNER, Juliane STEHLE, Daniel RAUH, Malte DRESCHER, 2020. Conformational selection vs. induced fit : insights into the binding mechanisms of p38α MAP Kinase inhibitors. In: Chemical Communications. Royal Society of Chemistry (RSC). 2020, 56(62), pp. 8818-8821. ISSN 1359-7345. eISSN 1364-548X. Available under: doi: 10.1039/d0cc02539aBibTex
@article{Roser2020-08-04Confo-50925, year={2020}, doi={10.1039/d0cc02539a}, title={Conformational selection vs. induced fit : insights into the binding mechanisms of p38α MAP Kinase inhibitors}, number={62}, volume={56}, issn={1359-7345}, journal={Chemical Communications}, pages={8818--8821}, author={Roser, Patrick and Weisner, Jörn and Stehle, Juliane and Rauh, Daniel and Drescher, Malte} }
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