Supplementary Fig. 1: Structural analysis of DRPB_Fz8-Fz8CRD complex.
From: Receptor subtype discrimination using extensive shape complementary designed interfaces
a, Titration original computation design (WT) and variants to Fz8CRD. The Phe42Ala and Thr66Ser point mutations to the original design (ptm9_5_1_5 in Supplementary Notes Table 1) are sufficient to confer binding to Fz8CRD. b, Titration of DRPB_Fz8 to biotinylated Fz 1/2/4/5/7/8 CRDs. DRPB_Fz8 was displayed on yeast surface. Biotinylated Fz 1/2/4/5/7/8 was added at different concentration. SA647 was subsequently added and the fluorescence data was analyzed and plotted in GraphPad Prism 7. DRPB_Fz8 showed strong binding to Fz5 and Fz8 whilst not interacting with Fz1, 2, 4 and 7 (Supplementary Notes Table 5). The yeast surface display titration has been repeated once with similar results. c, Structural superposition of DRPB_Fz8-Fz8CRD with XWnt8-Fz8CRD (PDB:4F0A). DRPB_Fz8 (light orange) and XWnt8 (magenta) are shown as cartoons. Fz8CRD (blue) is shown in surface representation. The lipid group of XWnt8 is shown as sticks. Zoomed view of the Fz8CRD hydrophobic groove showing steric clashes between DRPB_Fz8 “fingers” with XWnt8 lipid group. d, Phe42Ala mutations prevents steric clashes to neighboring residues.
