Figure 1

The intrinsic ATPase activity wild-type, R206H and G328V mutants of ACVR1 kinase domains with 0.5 mM ATP in pH 7.3 kinase buffer. (a) 22 oC and (b) 37 oC. The turnover rate kobs is quantified based on the ADP produced and normalized by the native ACVR1 concentration (see Methods). *p < 0.05, **p < 0.01, ***p < 0.001, unpaired t-test. (c) Coomassie stained SDS-PAGE gel of purified ACVR1 kinase domain stocks used for kinase assays. See Fig. S5 for the full-length gel image.