Protein tyrosine phosphatases: mechanisms of catalysis and regulation

https://doi.org/10.1016/S1367-5931(98)80095-1Get rights and content

Abstract

Recent structural information suggests that the HC(X)5R active-site motif defines three distinct evolutionary families of phosphatases that employ a common catalytic mechanism. In two instances, regulation of phosphatase activity employs autoinhibitory mechanisms involving either intermolecular or intramolecular interactions, whereby inhibition is mediated by sterically blocking the active-site cleft.

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