Tyrosine phosphatase

spinqualitylabelsall models Human tyrosine phosphatase 1B catalytic domain (grey) complex with EGFR peptide (in green), VO4, glycerol, Tris, 2-amino-2-hydroxymethyl-1,3-diol, 3i7z Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Tyrosine phosphatase or Protein tyrosine phosphatase (PTP) is an enzyme which removes phosphate from phosphorylated tyrosine residues. It is a key regulatory component of signal transduction pathways. 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. Human PTP PRL is found in regenerating liver. PTP class II are low molecular weight PTP (LMW-PTP) which dephosphorylate a number of growth factors and modulate their signalling processes. PTP class III contains CDC25 which removes phosphate from Thr and tyrosine. PTP containing SH2 domains are called PTP SHP. Yersinia PTP see Yersinia YopH. Non-receptor type PTPs are coded by the PTPN genes. T-cell PTP is a non-receptor type PTP expressed in hematopoietic tissues influencing most cells in the immune system. For details of PTP complex with inhibitor see Student Projects for UMass Chemistry 423 Spring 2012-9. Disease PTP mutations are involved in cancers. 3D Structures of tyrosine phosphatase Tyrosine phosphatase 3D structures

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