Fig. 1: Structural framework to describe cross-interactions of APR aggregation cores. | Nature Communications

Fig. 1: Structural framework to describe cross-interactions of APR aggregation cores.

From: Mapping the sequence specificity of heterotypic amyloid interactions enables the identification of aggregation modifiers

Fig. 1

a–c Three structural templates were generated for each APR amyloid core structure (shown in purple), corresponding to a self-elongation by monomeric APR addition (purple β-strands), b primary cross-interaction of a single position (highlighted in yellow) sequence variant (shown as green β-strands) at the amyloid fibril ends and c successive elongation by the same variant. d Variants that produce favourable differentials compared to monomeric APR elongation are driven towards heterotypic aggregation, compared to disfavourable potentials that limit interactions. Aggregation capping is instigated by sequences that are compatible to cross-interactions with the APR core but block further elongation, while opposite energies are associated to individual self-aggregation, respectively.

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