Insights derived from the structures of the Ser/Thr phosphatases calcineurin and protein phosphatase 1

AbstractThe crystal structures of serine/threonine phosphatases provide the basis for understanding their inhibition by physiologically relevant compounds such as microcystin, cyclosporin and FK506. The structures also highlight the importance of a common sequence motif found in a large family of metal-containing enzymes involved in phosphate ester hydrolysis