Polymodal allosteric regulation of Type 1 Serine/Threonine Kinase Receptors via a conserved electrostatic lock
Fig 8
Cartoon showing structure-function relationships in STKR1s.
Various kinase activity levels (inactive, leaky and active) are determined by two inhibitory mechanisms (FKBP12 binding and the endogenous R-D lock) and one activation mechanism (phosphorylation) that promotes FKBP12 dissociation, R-D lock disruption and also promotes substrate binding to the kinase domain.