Fig. 4: The interaction of PrP molecules in various PrP crystal structures.
From: Structural effects of the highly protective V127 polymorphism on human prion protein
a Superposition of human V127 (green), ovine30 (pink), rabbit31 (grey) and human D178N32 (yellow) PrP dimers from their respective crystal structures. Unlike V127, the other structures were obtained from apo-crystals in the absence of antibody. The ICSM18 antibody-binding epitope consists of α-helix 1 which is remote from the PrP dimer interface (see b and Supplementary Fig. 1). b Close up view of the β-sheet dimer interface common to the crystal dimers. The relative orientation of the two interacting PrP molecules in each structure differs depending on the intermolecular hydrogen-bonding patterns.
