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Issue 85, 2018
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Direct monitoring of the conformational equilibria of the activation loop in the mitogen-activated protein kinase p38α

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Abstract

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.

Graphical abstract: Direct monitoring of the conformational equilibria of the activation loop in the mitogen-activated protein kinase p38α

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Publication details

The article was received on 27 Jul 2018, accepted on 30 Sep 2018 and first published on 01 Oct 2018


Article type: Communication
DOI: 10.1039/C8CC06128A
Citation: Chem. Commun., 2018,54, 12057-12060
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    Direct monitoring of the conformational equilibria of the activation loop in the mitogen-activated protein kinase p38α

    P. Roser, J. Weisner, J. R. Simard, D. Rauh and M. Drescher, Chem. Commun., 2018, 54, 12057
    DOI: 10.1039/C8CC06128A

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