Predicted secondary and supersecondary structure for the serine-threonine-specific protein phosphatase family.
A bona fide consensus prediction for the secondary and supersecondary structure of the serine-threonine specific protein phosphatases is presented. The prediction includes assignments of active site segments, an internal helix, and a region of possible 3(10) helical structure. An experimental structure for a member of this family of proteins should appear shortly, allowing this prediction to be evaluated.
Jenny
T F
TF
Department of Chemistry, Swiss Federal Institute of Technology (E.T.H.), Zurich.
Gerloff
D L
DL
Cohen
M A
MA
Benner
S A
SA
D000595:Amino Acid Sequence; D001665:Binding Sites; D008961:Models, Structural; D008969:Molecular Sequence Data; D010749:Phosphoprotein Phosphatases / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D010749:Phosphoprotein Phosphatases