High resolution

Module 4: Figure structure of CaMKs

The domain structure and organization of Ca2+/calmodulin-dependent protein kinases (CaMKs).

The Ca2+/calmodulin-dependent protein kinases (CaMKs) share a number of similar domains. They all have an ATP-binding site (A), a catalytic domain (C) and an autoinhibitory domain (red) that overlaps the Ca2+/CaM (calmodulin)-binding domain (blue). Most of the CaMKs function as monomers, as shown for CaMKI at the bottom of the figure. In the resting state, the catalytic site (C) bends around to interact with the autoinhibitory domain (red). CaMKII is a multimeric enzyme, and half of the complex is illustrated on the right, where six monomers connect together through their C-terminal association domains to create a wheel-like structure (Module 4: Figure structure of CaMKII).