Figure 2 | Scientific Reports

Figure 2

From: Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease

Figure 2

Structural analysis of HuPrP(G127V) and WT HuPrP. (a,b) Cartoons of the 20 lowest-energy conformers for the mutant and WT proteins. (c,d) Details of the structural alteration at Tyr128 resulting from the G127V mutation (showing only dHε/Tyr128-Hγ/Ile182 and dHε/Tyr128-Hγ/Gln186 < 5.0 Å). (e,f) Distances (dαα, dαN, dNN < 5.0 Å) between the two strands (stretch-strands for G127V, β-strands for WT). (g,h) Local conformational alterations caused by the change of the dihedral angle psi(N-Cα-C-N) in Tyr157. These results demonstrate that the C-terminal structural cores of the mutant and WT proteins adopt different conformations.

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