Fig. 8: Perturbation of the R164 sidechain by V127 in V127 PrP crystals.
From: Structural effects of the highly protective V127 polymorphism on human prion protein
Comparison of residue 127, R164 and E168 side-chain positions in WT G127/M129 (cyan), V127/M129 (green) and V127/V129 PrP (yellow). Glycine 127 is coloured bright red, with the valine sidechains of residue 127 in V127/M129 and V127/V129 PrP coloured dark red. R164 and E168 in wild-type G127/M129 PrP are coloured dark blue, and lighter blue in both V127 variants. In both V127 variants the sidechain of R164 is sufficiently displaced from its position in the wild-type protein to significantly weaken the specific, strong (2.5 Å) hydrogen bonding interaction with E168 observed in wild-type G127/M129 PrP.
