The Structure and Topology of Protein Serine/Threonine Phosphatases

Structural studies of the two families of protein phosphatases responsible for dephosphorylating serine and threonine residues have revealed that, although these families are unrelated in sequence, the architecture of their catalytic domains is remarkably similar and distinct from the protein tyrosine phosphatases. The diversity of structure within the PPP and PPM families is generated by regulatory subunits and domains that function to modulate protein specificity and to localize the phosphatase to particular subcellular locations [1].