The potential of protein kinases as drug targets for a wide range of diseases is now well established. However, targeting kinases directly through competitive inhibitors poses a major selectivity challenge, as kinase active sites are typically quite conserved. A promising alternative strategy to inhibit kinases with enhanced selectivity relies on allosteric modulation. However, it is unclear how kinases integrate multiple concurrent allosteric signals and how protein dynamics influence the potencies and efficacies of allosteric drug leads. We will present our attempts to answer these fundamental questions for prototypical kinases.
12nd October 2022 ore 15.00, link zoom: https://uniroma1.zoom.us/j/88122875878?pwd=TZ7a7-lUpIUsw0mg5SuElkPnD_oRTc.1