Zn(II) binding causes interdomain changes in the structure and flexibility of the human prion protein.

ABSTRACT: The cellular prion protein (PrP^C) is a mainly α-helical 208-residue protein located in the pre- and postsynaptic membranes. For unknown reasons, PrP^C can undergo a structural transition into a toxic, β-sheet rich scrapie isoform (PrP^Sc) that is responsible for transmissible spongiform encephalopathies (TSEs). Metal ions seem to play an important role in the structural conversion. PrP^C binds Zn(II) ions and may be involved in metal ion transport and zinc homeostasis. Here, we use multiple biophysical techniques including optical and NMR spectroscopy, molecular dynamics simulations, and small angle X-ray scattering to characterize interactions between human PrP^C and Zn(II) ions. Binding of a single Zn(II) ion to the PrP^C N-ter

SUBMITTER: Gielnik M 

PROVIDER: S-EPMC8568922 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature