Figure 61.

HELL-F(209–277) amyloid fold presents strong similarity with HET-s (218–289), while the two prion domains lack in vivo cross-seeding. (a) Backbone structural alignment of the MAS NMR structures of the HELL-F (in blue) and HET-s (in yellow) prion-forming domains. (b,c) Four cartoons representing the hydrophobic triangular core of amyloid fibrils formed by the successively stacked pseudorepeats—R1 (left) and R2 (right)—of HELL-F (b) and HET-s (c). Hydrophobic residues are shown in white, acidic residues in red, basic residues in blue, and others in green. Reprinted with permission from ref (215). Copyright 2021 National Academy of Sciences of the USA.