Fig. 4: Comparison of the TDP-43 amyloid filament folds of type A FTLD-TDP and of ALS and type B FTLD-TDP.
From: TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP
a, Amino acid sequence alignment of the secondary structure elements of the TDP-43 filament folds of type A FTLD-TDP and of ALS and type B FTLD-TDP (PDB 7PY2). The N-terminal truncation site at P280 is indicated by a scissor symbol. R293 is indicated by a blue dot. b, Schematic of the secondary structure elements of the filament folds, shown for a single TDP-43 molecule perpendicular to the helical axis. Alternative local conformations of the type A FTLD-TDP filament fold are transparent, and R293 is highlighted. In a and b, arrows indicate β-strands. The glycine-rich (G274–G310, magenta), hydrophobic (M311–S342, white) and Q/N-rich (Q343–Q360, green) regions are highlighted.
