Skip to main content
. 2025 Jul 28;11(8):1628–1641. doi: 10.1038/s41477-025-02049-y

Fig. 4. PCA identifies amino acid properties contributing to expanded ligand perception.

Fig. 4

a, PCA of FLS2 homologues and their associated residue properties. The first five dimensions are displayed (dimensions (Dim.) 1 to 5) with their relative contributions across each FLS2 homologue. b, Highest ranked contribution of chemical residue variables for top two PCA dimensions. c, Heatmap of bulkiness (top), hydrophobicity (middle) and amino acid charge (bottom) along exposed residues of the LRR for different FLS2 variants. Residue swaps in synthetic variants that display differential bulkiness and/or charge are denoted (Δ bulkiness more than ±2, Δ hydrophobicity more than ±2, Δ charge more than ±0.5), with dark lines connected to the corresponding residue in the heatmaps. Surface-exposed residues are defined as ‘xLxxLxLxxNx’ of each LRR. d, AlphaFold3 model of the LRR regions of FLS2XL, VrFLS2, QvFLS2 and FcFLS2 with residues coloured by bulkiness or charge as labelled in c. Swaps of interest are outlined in black. At, Arabidopsis thaliana, Sl, Solanum lycopersicum. Ma, Manavalan; Mi, Miyazawa; Pa, Parker; Pr, Prabhakaran; Wo, Wolfenden.