Fig. 7: Truncations proximal to amino acid 400 destabilize PPM1D.
From: Allosteric inhibition of PPM1D serine/threonine phosphatase via an altered conformational state
A Distribution of PPM1D truncating mutations in solid tumor sequencing data from GENIE (v5.0) obtained from cBioportal (www.cbioportal.org). B Effects of different truncations on the thermal stability of PPM1D by differential scanning calorimetry. N = 3 independent sample runs. Data are presented as mean values ± SD. Source data are provided as a Source Data file. C Circular dichroism analysis of PPM1D1–420 (black), PPM1D1–400 (pink) and PPM1D1–377 (brown). D Relative differences in deuterium uptake between PPM1D1–420 and PPM1D1–400 (top) and between PPM1D1–420 and PPM1D1–377 (bottom) as assessed by HDX-MS. Vertical tick marks between peptides on the X-axis are shown to indicate regions of missing coverage. The bars below the X-axis represent the N-terminus (purple), loop (brown), hinge (cyan), flap (light purple), and C-terminus (black) of the protein.
