Skip to main content
. Author manuscript; available in PMC: 2022 Oct 27.
Published in final edited form as: Nature. 2022 Sep 15:10.1038/s41586-022-05319-3. doi: 10.1038/s41586-022-05319-3

Figure 2. Cryo-EM structure of α-synuclein filaments from Parkinson’s disease, Parkinson’s disease dementia and dementia with Lewy bodies (Lewy fold).

Figure 2

(a). Amino acid sequence of human α-synuclein. N-terminal region (residues 1-60) in orange, NAC region (residues 61-95) in green and C-terminal region (residues 96-140) in blue. Thick connecting lines with arrowheads indicate β-strands. (b). Cryo-EM density map and atomic model of the Lewy fold. The filament core extends from G31-L100. Islands A and B are indicated in grey. (c). Schematic of the Lewy filament fold of α-synuclein. Negatively charged residues are in red, positively charged residues in blue, polar residues in green, apolar residues in white, sulfur-containing residues in yellow and glycines in pink. Thick connecting lines with arrowheads indicate β-strands. Unknown residues are indicated by question marks.