Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation.
|Abstract||Long-term potentiation (LTP), a long-lasting enhancement in communication between neurons, is considered to be the major cellular mechanism underlying learning and memory. LTP triggers high-frequency calcium pulses that result in the activation of Calcium/Calmodulin (CaM)-dependent kinase II (CaMKII). CaMKII acts as a molecular switch because it remains active for a long time after the return to basal calcium levels, which is a unique property re ... [truncated at 450 characters in length]|
|Author||Rellos, Peter; Pike, Ashley C W; Niesen, Frank H; et al|
|Subject||Calcium Calcium-Calmodulin-Dependent Protein Kinase Type 2 Calmodulin Calorimetry Catalytic Domain Enzyme Activation Humans Isoenzymes Models, Molecular Phosphorylation Phosphothreonine Protein Binding Protein Multimerization Protein Structure, Quaternary Protein Structure, Secondary Substrate Specificity metabolism chemistry metabolism chemistry metabolism antagonists and inhibitors chemistry metabolism metabolism|