The calmodulin binding domain (blue highlight) of CaMKIV is located at the C-terminal helix of our model, immediately after the overlapping PP2A-binding and autoinhibitory domains. This domain binds to Calmodulin of the Calcium/calmodulin complex, and is essential for CaMKIV activation and the subsequent initation of the CaM Kinase pathway. Binding between Calcium/calmodulin complex and the calmodulin binding domain displaces the PP2A from the autoinhibitory domain to expose the activation loop of CaMKIV, which can be phoshosphorylated by CaMKK to produce autonomous CaMKIV activity.

Please note that the calmodulin binding domain is longer in the protein and that only a portion is shown here (the last 4 amino acids are not shown) due to the limitations implicated by the predicted model. The model depicts residues up to 337 th amino acid however the protein is composed of 473 residues.