Ontology highlight
ABSTRACT:
SUBMITTER: Damberger FF
PROVIDER: S-EPMC3198368 | biostudies-literature | 2011 Oct
REPOSITORIES: biostudies-literature
Damberger Fred F FF Christen Barbara B Pérez Daniel R DR Hornemann Simone S Wüthrich Kurt K
Proceedings of the National Academy of Sciences of the United States of America 20111010 42
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 16 ...[more]