Issue 85, 2018

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

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

Supplementary files

Article information

Article type
Communication
Submitted
27 Jul 2018
Accepted
30 Sep 2018
First published
01 Oct 2018

Chem. Commun., 2018,54, 12057-12060

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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements