Fig. 1: Illustrations of the Wnt/β-catenin pathway and the binding mode of β-catenin and a stapled peptide. | Nature Communications

Fig. 1: Illustrations of the Wnt/β-catenin pathway and the binding mode of β-catenin and a stapled peptide.

From: Design of target specific peptide inhibitors using generative deep learning and molecular dynamics simulations

Fig. 1

a Wnt signal on/off pathways. Cartoons were created with BioRender.com. b Crystal structure of a stapled peptide StAX-35R bound to β-catenin viewed from the N- or C-terminus of the peptide (PDBid: 4DJS32). c Helical length comparisons of the stapled peptide with the three interacting helices of β-catenin. d Correlation plots of I_bsa vs. I_sc and rmsALL_if vs. I_sc for 20 Rosetta Design generated N- or C-terminal extensions. For each peptide, 100 conformations were sampled, with each conformation represented by a scatter on the scatterplot. The sample sizes in (d) are n = 2000. Source data are provided as a Source Data file.

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