The Landscape of the Prion Protein's Structural Response to Mutation Revealed by Principal Component Analysis of Multiple NMR Ensembles
Figure 4
Comparative analysis of conformer plots, residue contribution, and structural interpolation of hPrP mutant NMR ensembles structures versus WT and variant hPrP.
Each row of the figure represents one PCA analysis and contains, from left to right, a conformer plot, residue contribution plot, and structural interpolation diagram. An explanation of the conformer plots is provided in Figure 1. Residue contribution to each PC is color-coded by PC (red = PC1, green = PC2, purple = PC3) in all residue contribution plots. For structural interpolation diagrams, PC1 is represented as equidistant atomic displacements from the mean structure (reference 1QLZ), and corresponding subdomains are indicated (red arrows). (A) Combined set of WT, variant and mutant hPrP NMR ensembles. The conformer plot is identical to Figure 1A. In the conformer plot, NMR ensembles of mutant structures are encircled in green, red, and blue ovals and labeled by their corresponding human disease, as well as the PDB code corresponding to the NMR ensemble (in brackets). The set of WT and variant hPrP structures (encircled by the black oval) have been labeled as WT+V. For rows (B–D), each analysis consists of the set of WT+V and an NMR ensemble from each of the CJD, FFI, and GSS mutant structures, respectively. The NMR ensemble of the mutant structure is encircled by an oval (color-coded to (A)), and labeled by the human disease it represents, and the PDB code corresponding to the NMR ensemble (in brackets). (B) CJD mutant (PDB 1FO7) and WT+V, (C) FFI mutant (PDB 2K1D) and WT+V, (D) GSS mutant (PDB 2KUN) and WT+V. (See also Figure S1).