Extended Data Fig. 8: Structures of α-synuclein protofilament cores.
From: Structures of α-synuclein filaments from multiple system atrophy
a, Schematic of secondary structure elements in the α-synuclein protofilament cores of MSA. Red arrows point to the non-proteinaceous density (in light red) at protofilament interfaces. b, c, Secondary structure elements in the α-synuclein protofilament cores assembled from recombinant wild-type (b) and mutant (c) α-synuclein. β-Strands are shown as thick arrows. d, Schematic depicting the first 100 amino acids of human α-synuclein, comparing secondary structure elements in protofilament cores from MSA with those in protofilament cores assembled from recombinant α-synuclein. As observed previously for tau filaments9, the arrangement of residues in β-strands is largely conserved among protofilament cores. This is especially the case for residues that adopt the conserved three-layered L-shaped motif, and less so for residues in the N-terminal arms.
