Tyrosine phosphatase

Tyrosine phosphatase (PTP) is an enzyme which removes phosphate from phosphorylated tyrosine residues. It is a key regulatory component of signal transduction pathways^[1]. PTPs are divided to 4 subfamilies. PTP class I contains receptor PTPs (RPTP) and dual-specificity PTP which removes phosphate from Ser/Thr and tyrosine. PTP class II are low moleculat weight PTP which dephosphorylate a number of growth factors and modulate their signalling processes^[2]. PTP class III contains CDC25 which removes phosphate from Thr and tyrosine. PTP containing SH2 domains are called PTP SHP. Non-receptor type PTPs are coded by the PTPN genes.
For details on Yersinia PTP see Yersinia YopH.
For details of PTP complex with inhibitor see Student Projects for UMass Chemistry 423 Spring 2012-9.

Disease

PTP mutations are involved in cancers^[3].

3D Structures of tyrosine phosphatase

Tyrosine phosphatase 3D structures