Skip to main content
Fig. 4 | Journal of Experimental & Clinical Cancer Research

Fig. 4

From: Flavokawain A is a natural inhibitor of PRMT5 in bladder cancer

Fig. 4

FKA binding to PRMT5 in BC cells. a The Glide docking method in Schrodinger software was used to predict the binding pattern between PRMT5 and FKA. The high-resolution docking model of FKA binding to PRMT5 was used to identify potential binding sites. b The Gaussian09 software package of Amber software was used to analyze the molecular dynamic simulations of FKA binding to PRMT5, and the corresponding RMSD (Upper) and RMSF (lower) scores were calculated. c Binding free energy analysis of FKA to amino acid residues of PRMT5. d Bio-layer interferometry detected the combination and dissociation process of FKA and human recombinant PRMT5 to determine the affinity between FKA and PRMT5. e Pull-down assays confirmed that biotin cross-linked FKA could precipitate with PRMT5 in 293 T cell lysis. f Confocal microscopy images indicate the co-localization of FKA with PRMT5 in T24 cells. PRMT5 (green fluorescence), FKA (red fluorescence), DAPI (blue fluorescence), and the merge images presents the integration of the three kinds of fluorescence

Back to article page