Figure 1

Figure 1

PAM and PLM can adopt a diverse range of conformations. (A) Protein multiple sequence alignment covering a region conserved between two canonical Wnt ligands (Wnt3 and Wnt8) of vertebrates and Wingless (Wg) of Drosophila. A conserved serine amino acid (red marked column with asterisk) has been shown to be acylated in various ligands. Consensus sequences are marked in green. Dr Danio rerio, Mm, Mus musculus, Dm, Drosophila melanogaster, and Xl Xenopus laevis. (B,C) Structurally characterized (B) PAM and (C) PLM conformations downloaded from PDB (depicted in white sticks) aligned on the backbone of 4F0A's fatty acid (represented in yellow sticks). (D) The probability density distributions of being conformationally close to 4F0A's ligand. The closeness measure used is the Root-mean-square deviation (RMSD) from 4F0A's ligand, calculated over its carbon atoms. Available PLM ligand conformers have a higher probability to be <1 Å away from 4F0A's ligand. The closest ligand to 4F0A's ligand is a PLM molecule, which is depicted as an inset.