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Fig. 2 | Journal of Experimental & Clinical Cancer Research

Fig. 2

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

Fig. 2

a Polar interactions formed by Arg 249 with neighbouring residues in p53WT. b Change in polar contacts with neighbouring residues due to mutation of Arg 249 to serine in p53R249S. b Superimposed view of the mutation site in p53WT and p53R249S. Residues of p53WT are shown in green and for p53R249S they are shown in pink. Change in the structure at 249th position is highlighted by a circle. Residues that acquired significantly different conformations are shown in stick representation. c Root mean square deviations of residues in p53WT and p53R249S. (a) RMSD of Arg 248 during the course of MD simulation in p53WT (green) and in p53R249S (red). (b) RMSD of residues from 249 to 271 in p53WT (green) and p53R249S (red)

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