Polymorphisms at Amino Acid Residues 141 and 154 Influence Conformational Variation in Ovine PrP
Figure 2
Ribbon diagrams that demonstrate structural features of ovine PrP. (a) Side-chain interactions in the vicinity of ovine PrP helix-1. Amino acid residue positions 141 and 154 are shown in magenta. Amino acid residue Arg154 that is present in the ALRQ allelic variant provides an extra interaction with Asp150. In contrast, the Phe141 in AFRQ and His154 in ALHQ interact with the aromatic stack that comprises amino acid residues Phe144, Tyr153, and Tyr160. (b) N-terminal β-sheet region of ALRQ. The structure of ALRQ forms an extended β-sheet comprising amino acid residues 112–121, β-strands 1 and 2 after mds.
