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. 2023 Jan 16;19(5):607–613. doi: 10.1038/s41589-022-01229-7

Fig. 5. Summary of structural differences between ME7 and RML prion protofibril structures.

Fig. 5

a, Licorice backbone models (ChimeraX) of ME7 and RML protofibrils colored according to PrPSc folding subdomains (blue, CC region; red, CV region; yellow, DS hairpin; white, intervening regions). Positive charge of the major basic patch (transparent surface) is indicated with + signs, and the sialoglycan occupancy corresponds to the intensity of red shading. The N-glycosylation sites (N180 and N196 side chains) and the disulphide bond are shown as sticks and colored by heteroatom (C, yellow; N, blue; O, red; S, yellow). b, Alignment of PrP sequences from different mammals focused on the PrPSc folding subdomains. Human residues 127 and 129 in the CV region (highlighted with dark red) are polymorphic (G/V and M/V, respectively).