Molecular mechanisms of theprotein serine/threonine phosphatases

doi:10.1016/S0968-0004(96)10060-8

Trends in Biochemical Sciences

Volume 21, Issue 11, November 1996, Pages 407-412

https://doi.org/10.1016/S0968-0004(96)10060-8 Get rights and content

The dephosphorylation of proteins on their serine, threonine and tyrosineresidues is catalysed by three families of protein phosphatases that regulate numerous intracellular processes. Diversity of structure within a family is generated by targeting and regulatory subunits and domains. Structural studies of these enzymes have revealed that although the two families of protein Ser/Thr phosphatases are unrelated in sequence, the architecture of their catalytic domains is remarkably similar and distinct from the protein tyrosine phosphatases. Insights into the molecular mechanisms of catalysis and regulation of these enzymes have been obtained.

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¹: D. Barford is at the Laboratory of Molecular Biophysics, University of Oxford, Rex Richards Building, South Parks Road, Oxford, UK OX1 3QU

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Trends in Biochemical Sciences

Molecular mechanisms of theprotein serine/threonine phosphatases

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