Supplementary Figure 3: Full-length structure of the α-syn fibril, illustrating important features in expanded regions.
From: Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
(a) View along the fibril axis showing the highly ordered core and the disordered tails. (b) Side view showing the β-sheet packing between each monomer as well as the disordered tails. (c-f) Core interactions illustrating NMR distance restraints with dotted lines. (g-l) Backbone traces for neighboring monomers drawn in blue, yellow, orange and red. (g, h) Side and top views of the salt bridge from E46 to K80 of the neighboring monomer. (i, j) Side and top views of the I88-A91-F94 pocket perpendicular to the fibril axis, exhibiting short intermolecular distances. (k, l) Side and top view of the Q79 side chain exhibiting a glutamine ladder, with intermolecular hydrogen bonds involving Nɛ2 and Oɛ1 moieties.
