Open access
Oct 2026
Crystal structure of activated MAPKAPK2 kinase reveals a C-lobe allosteric pocket for furan-2-carboxamide inhibitors
It is shown through isothermal titration calorimetry that MK-25 binds the activated MAPKAPK2, consistent with state-dependent allosteric binding, and a ligandable allosteric pocket is identified that may facilitate future structure-guided design of selective, non-ATP-competitive MAPKAPK2 inhibitors.
E. Beaumont, S. Duclos, S. Thieffine et al.
· bioRxiv · 0 citations