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Yersinia protein tyrosine phosphatase YopH

Hu, X., Stebbins, C. E. Molecular Docking and 3D QSAR Studies of Yersinia Protein Tyrosine Phosphatase YopH Inhibitors. Bioorg. Med. Chem. 2005, 13, 1101-1109. [Pg.248]

Hu X, Stebbins CE. Molecular docking and 3D-QSAR studies of Yersinia protein tyrosine phosphatase YopH inhibitors. Bioorg. Med. Chem. 2005 13 1101-1109. [Pg.2046]

The PTPs catalyze the hydrolysis of phosphorylated tyrosine residues in proteins, to yield the free tyrosine side chains and inorganic phosphate. They are classified according to substrate specificity (1) tyrosine-specific PTPs, such as the Yersinia PTP (YopH) and the mammalian PTPIB and PTPl, which in vivo hydrolyze only pTyr residues as well as (2) the dual-specificity phosphatases (DSPs), such as the human VHR and Cdc25, which hydrolyze pTyr and pSer and pThr residues of protein substrates. Based on their cellular localization, PTPs are classified as receptor-like or intracellular. ... [Pg.331]


See other pages where Yersinia protein tyrosine phosphatase YopH is mentioned: [Pg.233]    [Pg.233]    [Pg.23]   
See also in sourсe #XX -- [ Pg.233 ]




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