Published In
Nature Communications
Document Type
Article
Publication Date
6-7-2017
Subjects
Protein kinases, Electron microscopy, Enzymes -- Structure
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
DOI
10.1038/ncomms15742
Persistent Identifier
http://archives.pdx.edu/ds/psu/20383
Citation Details
Myers, J. B., Zaegel, V., Coultrap, S. J., Miller, A. P., Bayer, K. U., & Reichow, S. L. (2017). The CaMKII holoenzyme structure in activation-competent conformations. Nature communications, 8, 15742.
Description
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Copyright The Author(s) 2017