The CaMKII holoenzyme structure in activation-competent conformations

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

Nature Communications, 2017, vol. 8, issue 1, 1-15

Abstract: Abstract The Ca2+/calmodulin-dependent protein kinase II (CaMKII) assembles into large 12-meric holoenzymes, which is thought to enable regulatory processes required for synaptic plasticity underlying learning, memory and cognition. Here we used single particle electron microscopy (EM) to determine a pseudoatomic model of the CaMKIIα holoenzyme in an extended and activation-competent conformation. The holoenzyme is organized by a rigid central hub complex, while positioning of the kinase domains is highly flexible, revealing dynamic holoenzymes ranging from 15–35 nm in diameter. While most kinase domains are ordered independently, ∼20% appear to form dimers and

Date: 2017
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15742

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DOI: 10.1038/ncomms15742

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