Extended Data Fig. 4: Molecular dynamics simulations show overlapping structural changes of POM1-PrPC complex and pathogenic PRNP mutations.
From: A conformational switch controlling the toxicity of the prion protein
Extended Data Figure 4. (a) MD simulations of POM1 binding and pathogenic PRNP mutations causing genetic prion disease show the R156-E196 interaction is abolished and induction of the H140-R208 H-latch is established. Each datapoint represents one independent simulation, values are given as mean ± standard deviation. (b) In agreement with this view, POM1 and human, hereditary PrP mutations responsible for fatal prion diseases favor altered flexibility in the α2-α3 and β2-α2 loop.
