Fig. 5: The CaMKIIα-0 holoenzyme is comprised of domain-swapped dimers.
From: A domain-swapped CaMKII conformation facilitates linker-mediated allosteric regulation
A Surface representation of CaMKIIδ holoenzyme crystal structure (PDB code: 8USO) in two perspectives showing the interaction between the kinase domain of one subunit and the hub domain of another subunit. B The connector segments (defined as residues 305–314) in the CaM footprints of two domain-swapping subunits are shown as sticks. The kinase domain of subunit B has been omitted for clarity.
