Ontology highlight
ABSTRACT:
SUBMITTER: Myers JB
PROVIDER: S-EPMC5467236 | biostudies-literature | 2017 Jun
REPOSITORIES: biostudies-literature
Myers Janette B JB Zaegel Vincent V Coultrap Steven J SJ Miller Adam P AP Bayer K Ulrich KU Reichow Steve L SL
Nature communications 20170607
The Ca<sup>2+</sup>/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 domai ...[more]