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. 2022 Feb 11;31(14):2348–2357. doi: 10.1093/hmg/ddac037

Figure 2.

Figure 2

The R914W mutation is a functional null mutation. (A) Image showing the hydrogen-binding contacts (dashed lines) of R914 in the intracellular domain of PDGFRA. R914 and all interacting amino acids are labeled. Individual red circles are water molecules from the solvent. Image from the RCSB PDB (rcsb.org) of PDB 5K5X (18). (B) Schematic showing the domain structure of PDGFRA. Key domains and tested mutations are shown. IgL, immunoglobulin-like domains; JM, juxta-membrane domain; TK #1, tyrosine kinase domain 1; TK #2, tyrosine kinase domain 2. (C) Summary of flow cytometry data measuring the responsiveness (total EGFP signal) of the receptors to PDGF ligands. The horizontal dashed line indicates the baseline signal (WT receptor, no ligand). Data shown are the means ± SD of three independent biological replicate experiments. The results were evaluated using two-way ANOVA (alpha = 0.05) and all tested variables show a P-value < 0.0001 (Supplementary Material, Tables S9 and S10).