Crystal structures of catalytic and regulatory subunits of rat protein kinase CK2.

Protein kinase CK2 consists of two catalytic subunits (CK2α) and two regulatory subunits (CK2β). Here, we report the crystal structures of rat CK2α mutant (rCK2α-ΔC, 1-335) and CK2β (rCK2β). The overall topology of rCK2α-AC and rCK2β are very similar to the human enzyme, although large structural differences could be observed in the N-terminal domain of rCK2α-AC. Our reported structure of rCK2α-AC is in the close conformation state while the counterpart hCK2α is in the open conformation state, indicating the conformation of CK2α molecule has high plasticity. The structure of rCK2β represents the conformation of free CK2β. Upon CK2β binding, the C-terminal region undergoes a drastic conformational change. The major region of interaction within the interface of CK2α/CK2β may serve as a bridge to transmit the conformational change and thus regulate the activity of CK2α. [ABSTRACT FROM AUTHOR]