A specific amino acid context in EGFR and HER2 phosphorylation sites enables selective binding to the active site of Src homology phosphatase 2 (SHP2)
Zachary Hartman, Werner J. Geldenhuys, Yehenew M. Agazie
Abstract
and EGFR and HER2 signaling in cells, suggesting inhibition of SHP2 protein tyrosine phosphatase activity by this peptide. Although we do not expect this peptide to be a strong inhibitor by itself, we foresee that the insights into SHP2 selectivity described here will be useful in future development of active-site small molecule-based inhibitors.
Topics & Concepts
Proto-oncogene tyrosine-protein kinase SrcPhosphorylationBinding siteActive sitePhosphataseHomology (biology)Context (archaeology)ChemistryBiologyComputational biologyAmino acidBiochemistryCell biologyEnzymePaleontologyProtein Tyrosine PhosphatasesGalectins and Cancer BiologyGlycosylation and Glycoproteins Research