High resolution

Module 4: Figure structure of CaMKII



Three-dimensional structure of Ca2+/calmodulin-dependent protein kinase II (CaMKII).

The domain structure at the bottom illustrates the different structural regions of one of the Ca2+/calmodulin-dependent protein kinase (CaMKII) monomers that make up the dodecameric structure. The structure of the multimeric holoenzyme was determined by reconstructing electron microscopic images. It has a barrel-shaped structure made up of the association domains forming the inner core, with the catalytic domains protruding as foot structures from either side. In effect, there will be a ring of six catalytic domains on either side of the molecule that are located close enough for the intermolecular interactions necessary for enzyme activation (Module 4: Figure CaMKII activation). The stain model-based reconstructions were reproduced from Kolodziej, S.J., Hudmon, A., Waxham, M.N. and Stoops, J.K. (2000) Three-dimensional reconstructions of calcium/calmodulin-dependent (CaM) kinase IIa and truncated CaM kinase IIa reveal a unique organisation for its structural core and functional domains. J. Biol. Chem. 275:14354–14359, with permission from the American Society for Biochemistry and Molecular Biology; see Kolodziej et al. 2000.