Fig. 3: β-strand configuration of native PMEL amyloid. | Nature Communications

Fig. 3: β-strand configuration of native PMEL amyloid.

From: Cryo-EM of wild-type and mutant PMEL amyloid cores reveals structural mechanism of pigment dispersion syndrome

Fig. 3

a Ribbon diagrams of native PMEL amyloid fibrils, illustrating the four-layered structure of β-strands in the fibril core. b Amino acid sequence of the N-terminal portion of the CAF domain, with the positions of β-strands (indicated by arrows) predicted using ModelAngelo. c Close-up views of the parallel cross-β sheets, highlighting the structural differences between wild-type and G175S mutant fibrils. Insets (left) show cross-sectional views of the fibril core to indicate the positions of the β-sheets (boxes). In the G175S mutant, Thr155 (box, left) separates β1-1 and β1-2, resulting in the division of the β-sheet. Note the alignment of aromatic residues along the fibril axis, emphasizing the positioning of these bulky residues in both wild-type and G175S mutant fibrils. Panel (c) highlights intra-protofilament interactions along the fibril axis, which are maintained primarily through backbone hydrogen bonding between stacked β-strands. Carbon: green; oxygen: red; nitrogen: blue; sulfur: yellow.

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