Role of Tyrosine Phosphorylation in PTP–PEST

We\nstudy the influence of tyrosine phosphorylation on PTP–PEST,\na cytosolic protein tyrosine phosphatase. Utilizing a combination\nof experimental data and computational modeling, specific tyrosine\nsites, notably, Y64 and Y88, are identified for potential phosphorylation.\nPhosphorylation at these sites affects loop dynamics near the catalytic\nsite, altering interactions among key residues and modifying the size\nof the binding pocket. This, in turn, impacts substrate binding, as\nindicated by changes in the binding energy. Our findings provide insights\ninto the structural and functional consequences of tyrosine phosphorylation\non PTP–PEST, enhancing our understanding of its effects on\nsubstrate binding and catalytic conformation.