Find in Library

Together with protein tyrosine kinases (PTKs), protein tyrosinephosphatases (PTPs) serve as hallmarks in cellular signaltransduction by controlling the reversible phosphorylation oftheir substrates. The human genome is estimated to encodemore than 100 PTPs, which can be divided into elevensub-groups according to their structural and functionalcharacteristics. All the crystal structures of catalytic domains ofsub-groups have been elucidated, enabling us to understandtheir precise catalytic mechanism and to compare theirstructures across all sub-groups. In this review, I describe thestructure and mechanism of catalytic domains of PTPs in thestructural context.