Additional file 1: of Wild type p53 function in p53Y220C mutant harboring cells by treatment with Ashwagandha derived anticancer withanolides: bioinformatics and experimental evidence

Table S1. PDB IDs of different p53 protein variants and their structural resolution. Table S2. H-bond network around residue 249 in p53WT and p53R249S. Table S3. Binding score of Wi-A and Wi-N with different p53 mutants of DNA binding site. Table S4. Docking scores (XP docking) of withanolides and PhiKan with p53WT and p53Y220C. Figure S1. Three domains of p53 protein. The structure of p53 contains N-terminal, central domain and C-terminal. Figure S2. (A) Immunostaining of control and Wi-A treated cells with anti-p53 antibodies detecting the total protein and mutant p53 specifically. Both antibodies detected the p53 protein in MRC-5hTERT p53V143A and MRC-5hTert p53Y220C showed decrease in p53 staining in the nucleus. Quantitation of total and mutant p53 from immunostaining images is shown in (B) and (C), respectively. Figure S3. (A) Immunostaining of control and doxorubicin (a DNA damage inducing reagent) treated cells with anti-53BP1 and p21WAF-1 antibodies. Increase in 53BP1 and p21WAF-1 was observed in treated cells. Quantitation of 53BP-1 and p21WAF1 from immunostaining images is shown in (B) and (C), respectively. Figure S4. Quantitation of immunostaining images of mortalin (A) and p53 (B) shown in Fig. 5; p21WAF1 and HP1g (shown in Fig. 6) and p53 (shown in Fig. 7). (PDF 8692 kb