Identification of putative druggable pockets in PRL3, a significant oncology target, using in silico analysis

Abstract

Aberrant cellular phosphorylation is a hallmark of several diseases including inflammation and cancers (1–3). Protein phosphorylation is a post-translational modification that can act as a switch to regulate biochemical pathways and is regulated by the concerted action of two classes of enzymes: kinases and phosphatases. As such, kinases and phosphatases present as significant potential clinical molecular targets. To date, several kinase inhibitors have been approved for various indications and kinases have been regarded as one of the most important drug targets of the 21st century (4–8). Meanwhile, phosphatases are recently gaining traction as therapeutic drug targets, particularly with emerging roles in cancers (9–12). Development of phosphatase inhibitors offer a novel approach to treatment of diseases involving dysregulated protein phosphorylation.