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
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.