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Unraveling the key to the resistance of canids to prion diseases

Fig 4

Electrostatic potentials on the surface of protein structures.

A. Wild-type mouse prion protein (PDB ID: 4MA7). B. Canine prion protein (PDB ID: 1XYK). C-E. Modelled structures: Model01 (C), Model02 (D), and distribution of positively charged residues surrounding Asp158 in wild-type canine prion protein (E). Acidic regions are colored in red and basic regions in blue, residue 158 for all structures is highlighted in dashed line white box. Amino acid D158 located within an area with four Arg/Lys residues (R135, R150, R155 and K119) introduces a positively charged residue in that region, in dog PrP, Model01 and Model02 changing the local charge distribution compared to mouse wild-type PrP.

Fig 4

doi: https://doi.org/10.1371/journal.ppat.1006716.g004