Calcium-dependent serine/threonine phosphatase (also known as protein phosphatase 2B or PP2B).
Calcineurin is a heterodimer composed of a catalytic subunit (Calcineurin A) and a regulatory subunit that contains an autoinhibitory domain (Calcineurin B). The catalytic subunit also contains a calmodulin-binding domain. Binding of calcium to the regulatory sununit allows the binding of calmodulin to the catalytic subunit, resulting in displacement of the autoinhibitory domain and enzymatic activation.
Calcineurin has many functions within eukaryote cells but is best known for its role in activating transcription of the interleukin 2 (IL-2) gene. IL-2 is required for activation of B- and T- cells and thus calcineruin inhibitors such as cyclosporin A and FK506, are potent immunosuppressants.