Fig. 3: Structure comparison of G51D, WT1a, and E46K fibrils.
From: The hereditary mutation G51D unlocks a distinct fibril strain transmissible to wild-type α-synuclein
a Overlay of the structures of every single α-syn subunit from the G51D, E46K, and WT1a fibrils. G51D fibril is in green; WT1a fibril is in slate; E46K fibril is in pink. The region with a similar structure shared by three different FC is circled on topology diagrams. b Rearrangement of α-syn fibril structure triggered by G51D mutation. Residues involved in the protofilament interfaces are presented in spheres. The protofilament interface of WT1a fibril is colored in cyan; the interface of the G51D fibril is colored in orange. D51 and G51 are highlighted in red. E46 and K46 are in purple. c Zoom-in views of the WT1a and G51D fibril interfaces. d The β-hairpin (residues 50–66) formed in the G51D fibril structure is zoomed in with D51 in red. e Overlay of the structures of every single α-syn subunit from the G51D and E46K fibrils. G51D mutation disrupts the β-turn formed of residues 45–57 formed in the E46K fibril. G51 and D51 are highlighted in red. K46 is highlighted in purple.
