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- W2155292205 abstract "In the otherwise highly conserved NMR structures of cellular prion proteins (PrP C ) from different mammals, species variations in a surface epitope that includes a loop linking a β-strand, β2, with a helix, α2, are associated with NMR manifestations of a dynamic equilibrium between locally different conformations. Here, it is shown that this local dynamic conformational polymorphism in mouse PrP C is eliminated through exchange of Tyr169 by Ala or Gly, but is preserved after exchange of Tyr 169 with Phe. NMR structure determinations of designed variants of mouse PrP(121–231) at 20 °C and of wild-type mPrP(121–231) at 37 °C together with analysis of exchange effects on NMR signals then resulted in the identification of the two limiting structures involved in this local conformational exchange in wild-type mouse PrP C , and showed that the two exchanging structures present characteristically different solvent-exposed epitopes near the β2–α2 loop. The structural data presented in this paper provided a platform for currently ongoing, rationally designed experiments with transgenic laboratory animals for renewed attempts to unravel the so far elusive physiological function of the cellular prion protein." @default.
- W2155292205 created "2016-06-24" @default.
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- W2155292205 date "2011-10-10" @default.
- W2155292205 modified "2023-09-25" @default.
- W2155292205 title "Cellular prion protein conformation and function" @default.
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- W2155292205 doi "https://doi.org/10.1073/pnas.1106325108" @default.
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