Supplementary Figure 8: Detailed analysis of the R-shaped fold.
From: Cryo-EM structures of four polymorphic TDP-43 amyloid cores
a, (Left column, from top to bottom) Cross-section of three layers of the homodimer and heterodimer interfaces in SegB A315E are shown. Side view of the detailed interactions of each interface are shown in the right columns. b, Side view of hydrophilic interactions in the head of the R-shaped fold in the SegB A315E. c, Superposition of SegA and SegB A315E main chain models shows TDP-43 cannot simultaneously form a dagger-shaped fibril and an R-shaped fibril because of steric clashes; it must form either one or other. The simplified comparison using only SegA-sym to represent the dagger-shaped fold and SegB A315E inner chain to represent the R-shaped fold is shown in the right panel. Color coding in this figure is the same as in Fig. 2, hydrogen bonds with distance between 2.3–3.2 Å are shown as black dashed lines. (Detailed alignment parameters are listed in Supplementary Table 2).
