Polymodal allosteric regulation of Type 1 Serine/Threonine Kinase Receptors via a conserved electrostatic lock
Fig 9
Inactive STKR1 adopts a conformation similar to that of the fully active kinases.
(a). Comparison between active and inactive A-loop conformation between STKR1 (ALK5), cyclin-dependent kinase (CDK). (b). Representative inactive FKBP12-ALK2WT catalytic site conformation from MD simulations, with K-E and R-D salt bridge highlighted. R-spine is shown in vdW surface mode colored by atom type. (c). Comparison of DLG-in with DFG-in conformation. DFG motif from Src is shown in licorice mode and GLG motif and R375 are shown in CPK mode.