Protein serine/threonine phosphatases.
In the past year, the three-dimensional structures of two serine/threonine phosphatases, protein phosphatase-1 and protein phosphatase-2b (calcineurin), have been determined. The new information puts previous sequence comparisons and mutagenesis studies into a detailed structural perspective. The active-site structure and catalytic mechanism appear to be common to a variety of phosphoesterase enzymes.
Villafranca
J E
JE
Agouron Pharmaceuticals Inc., La. Jolla, CA 92037, USA. ern@agouron.com
Kissinger
C R
CR
Parge
H E
HE
D000595:Amino Acid Sequence; D019703:Calcineurin; D002148:Calmodulin-Binding Proteins / Q000737:chemistry / Q000235:genetics; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010749:Phosphoprotein Phosphatases / Q000737:chemistry* / Q000145:classification / Q000235:genetics / Q000502:physiology*; D011487:Protein Conformation; D015202:Protein Engineering; D054645:Protein Phosphatase 1; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012694:Serine / Q000378:metabolism; D013912:Threonine / Q000378:metabolism
D002148:Calmodulin-Binding Proteins; D011994:Recombinant Proteins; D013912:Threonine; D012694:Serine; D019703:Calcineurin; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1