Acvr1c^tm3Cfi

Two mutations, a leucine to valine change at amino acid 250 (p.L250V) in exon 4 and an a serine to glycine change at amino acid 270 (p.S270G) in exon 5 were introduced in the active site of the kinase. Substitution of the gatekeeper residue Ser270 with Gly creates an extra pocket in the active site, which is further expanded by mutating the adjacent residue Leu250 to Val. These mutations render the mutant receptor sensitive to inhibition by ATP competitive inhibitors, such as 2NaPP1. (J:269067)