Fig. 6: Disease mutations alter the structure of D10 and D2 amyloid fibrils.
From: Amyloid fibril structures link CHCHD10 and CHCHD2 to neurodegeneration
a Stick representation of the cryo-EM structures of a single layer of the ordered fibril core of S59L D10-NT fibrils. Residue L59 is shown in red. Beta strands are highlighted in yellow. b Stick representation of the cryo-EM structures of a single layer of the ordered fibril core of the T61I D2-NT fibrils. Residue I61 is shown in red. Beta strands are highlighted in yellow. c ThT monitored aggregation of purified recombinant WT (black), S59L (red), and R15L (blue) D10-NT. d ThT T50 for WT, S59L and R15L D10-NT assembly (mean ± SD, n = 3 biological replicates, unpaired two-tailed paramettric Student’s t-test; ns p = 0.060, * p = 0.045, ** p = 0.003). e Overlayed NMR 15N-1H HSQC spectra of S59L (red) and WT (black) D10-NT (see Supplementary Fig. 17 for a full-page version). f Ratios of S59L D10-NT NMR resonance intensities to those of corresponding WT D10-NT resonance intensities. g ThT monitored aggregation of purified recombinant WT (black) and T61I (orange) D2-NT. Data for WT D2-NT are the same as in Fig. 2a. h ThT T50 for WT and T61I D2-NT assembly (mean ± SD, n = 3 biological replicates, unpaired two-tailed parametric Student’s t-test; p = 0.26. i Overlayed NMR 15N-1H HSQC spectra of T61I (orange) and WT (black) D2-NT (see Supplementary Fig. 18 for a full-page version). j Ratios of T61I D2-NT NMR resonance intensities to those of corresponding WT D12-NT resonance intensities. Source data for c, d, f–h, j are provided as a Source Data file.
