The CaMKII holoenzyme structure in activation-competent conformations

Janette B. Myers; Vincent Zaegel; Steven J. Coultrap; Adam P. Miller; K. Ulrich Bayer; Steve L. Reichow

doi:10.1038/ncomms15742

Nature Communications (Jun 2017)

The CaMKII holoenzyme structure in activation-competent conformations

Janette B. Myers,
Vincent Zaegel,
Steven J. Coultrap,
Adam P. Miller,
K. Ulrich Bayer,
Steve L. Reichow

Affiliations

Janette B. Myers: Department of Chemistry, Portland State University
Vincent Zaegel: Department of Pharmacology, University of Colorado
Steven J. Coultrap: Department of Pharmacology, University of Colorado
Adam P. Miller: Department of Chemistry, Portland State University
K. Ulrich Bayer: Department of Pharmacology, University of Colorado
Steve L. Reichow: Department of Chemistry, Portland State University

DOI: https://doi.org/10.1038/ncomms15742
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 15

Abstract

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Ca2+/calmodulin-dependent protein kinase II (CaMKII) forms a 12 subunit holoenzyme central to synaptic plasticity. Here the authors report a 3D structure of the CaMKII holoenzyme in an activation-competent state obtained by single particle EM, and suggest a role for the intrinsically disordered linker domain in facilitating cooperative activation.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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