Fig. 8
From: Tau local structure shields an amyloid-forming motif and controls aggregation propensity
Molecular model of tau amyloid domain structural rearrangement and subsequent aggregation. Naive tau monomer (left) exists with a propensity to form a relatively collapsed structure, which buries the amyloid domain 306VQIVYK311. In the presence of disease-associated mutations, proline isomerization events, or certain splice isoforms, the equilibrium is shifted to disfavor local compact structure. This exposes the aggregation-prone 306VQIVYK311 amyloid motif and enhances aggregation propensity, leading to subsequent tau pathology
