Ontology highlight
ABSTRACT:
SUBMITTER: Apostol MI
PROVIDER: S-EPMC3766960 | biostudies-literature | 2013 Jul
REPOSITORIES: biostudies-literature
Journal of the American Chemical Society 20130702 28
The structural transition of the prion protein from α-helical- to β-sheet-rich underlies its conversion into infectious and disease-associated isoforms. Here we describe the crystal structure of a fragment from human prion protein consisting of the disulfide-bond-linked portions of helices 2 and 3. Instead of forming a pair-of-sheets steric zipper structure characteristic of amyloid fibers, this fragment crystallized into a β-sheet-rich assembly of hexameric oligomers. This study reveals a never ...[more]