Insights derived from the structures of the Ser/Thr phosphatases calcineurin and protein phosphatase 1.
The 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.
Lohse
D L
DL
Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor 48109-0606, USA.
Denu
J M
JM
Dixon
J E
JE
D000595:Amino Acid Sequence; D019703:Calcineurin; D002148:Calmodulin-Binding Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry*; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D016572:Cyclosporine / Q000494:pharmacology; D052998:Microcystins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010456:Peptides, Cyclic / Q000737:chemistry / Q000378:metabolism; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D011487:Protein Conformation; D054645:Protein Phosphatase 1; D016559:Tacrolimus / Q000494:pharmacology
D002148:Calmodulin-Binding Proteins; D052998:Microcystins; D010456:Peptides, Cyclic; C078588:microcystin; D016572:Cyclosporine; D019703:Calcineurin; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1; D016559:Tacrolimus