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

Structure. 1995 Oct 15;3(10):987-90. doi: 10.1016/s0969-2126(01)00234-9.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Calcineurin
  • Calmodulin-Binding Proteins / antagonists & inhibitors
  • Calmodulin-Binding Proteins / chemistry*
  • Conserved Sequence
  • Crystallography, X-Ray
  • Cyclosporine / pharmacology
  • Microcystins
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Peptides, Cyclic / chemistry
  • Peptides, Cyclic / metabolism
  • Phosphoprotein Phosphatases / antagonists & inhibitors
  • Phosphoprotein Phosphatases / chemistry*
  • Protein Conformation
  • Protein Phosphatase 1
  • Tacrolimus / pharmacology

Substances

  • Calmodulin-Binding Proteins
  • Microcystins
  • Peptides, Cyclic
  • microcystin
  • Cyclosporine
  • Calcineurin
  • Phosphoprotein Phosphatases
  • Protein Phosphatase 1
  • Tacrolimus