All-atom simulation of the HET-s prion replication
Fig 3
Structure of the HET-s Prion Forming Domain in the amyloid form.
Lateral (A) and top (B) view of a HET-s amyloid trimer retrieved from PDB 2KJ3. Each monomer of the fibril displays a 2-Rung-β-Solenoid conformation. The N-terminal rung (residues 225–245) is depicted in blue, while the C-terminal rung (residues 261–281) is depicted in red. The colored bar at the left represents the polarity (N to C, blue to red) of the fibril.