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The researchers discovered that PKC's calcium-sensing domain interacts with its own tail and enzymatic domain , locking the enzyme in an inactive pose. PKC begins to activate when calcium triggers the bridging of the C2 domain to the cell membrane, starting the enzyme intended for activity thus. The team also validated this packing by mutating specific parts of the proteins that hold the domains together, unlocking and relocking PKC between unpacked and properly packed structures. Knowing the interfaces that keep PKC closed will today permit the design of small molecules that may either disrupt the interactions between PKC's domains to start and activate the enzyme, or clamp the domains closed to prevent its activation, said first writer Corina Antal, PhD, who was a graduate student in Newton's laboratory during the scholarly study..