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. Author manuscript; available in PMC: 2018 Sep 5.
Published in final edited form as: Biochemistry. 2017 Aug 21;56(35):4637–4645. doi: 10.1021/acs.biochem.7b00638

Figure 4.

Figure 4

Inhibition of Sts-1HP. A set of known phosphatase inhibitors (A) were screened for their capacity to inhibit the phosphatase activity of Sts-1HP. The SHP-1 inhibitor, PHPS1, was shown to be a potent competitive inhibitor of Sts-1HP (B, Ki of 1.05 ± 0.15 μM). Shown is a Lineweaver-Burk plot of the activity of Sts-1HP (as measured by pNPP assay) with three different concentrations of the inhibitor, PHPS1. Examination of the structure of Sts-1HP shows that there is a clear binding cleft where the substrates and inhibitors bind (C, Sts-1HP shown in surface representation colored red, the conserved histidine residues are colored blue while the conserved arginine residues are colored grey).