Ontology highlight
ABSTRACT:
SUBMITTER: Hosszu LLP
PROVIDER: S-EPMC7391680 | biostudies-literature | 2020 Jul
REPOSITORIES: biostudies-literature
Hosszu Laszlo L P LLP Conners Rebecca R Sangar Daljit D Batchelor Mark M Sawyer Elizabeth B EB Fisher Stuart S Cliff Matthew J MJ Hounslow Andrea M AM McAuley Katherine K Leo Brady R R Jackson Graham S GS Bieschke Jan J Waltho Jonathan P JP Collinge John J
Communications biology 20200729 1
Prion diseases, a group of incurable, lethal neurodegenerative disorders of mammals including humans, are caused by prions, assemblies of misfolded host prion protein (PrP). A single point mutation (G127V) in human PrP prevents prion disease, however the structural basis for its protective effect remains unknown. Here we show that the mutation alters and constrains the PrP backbone conformation preceding the PrP β-sheet, stabilising PrP dimer interactions by increasing intermolecular hydrogen bo ...[more]