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Related Experiment Videos

Prion protein selectively binds copper(II) ions

J Stöckel1, J Safar, A C Wallace

  • 1Department of Neurology, University of California, San Francisco 94143-0518, USA.

Biochemistry
|June 4, 1998
PubMed
Summary
This summary is machine-generated.

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Copper ions bind specifically to the prion protein (PrP), influencing its structure and potentially its normal function. This interaction involves copper binding to octarepeat regions, suggesting a role in PrP

Area of Science:

  • Biochemistry
  • Neuroscience
  • Structural Biology

Background:

  • The physiological function of cellular prion protein (PrPC) is largely unknown.
  • PrPC undergoes structural changes to form the infectious PrPSc isoform.
  • Understanding PrPC's normal role is crucial for deciphering prion diseases.

Purpose of the Study:

  • To investigate metal ions as potential ligands for the prion protein.
  • To elucidate the structural impact of metal ion binding on PrPC.
  • To explore the role of copper in PrP structure and function.

Main Methods:

  • Recombinant Syrian hamster prion protein (SHaPrP(29-231)) was used.
  • Near-UV circular dichroism (CD) spectroscopy assessed protein conformation.
  • Tryptophan fluorescence spectroscopy monitored structural changes upon metal binding.

Related Experiment Videos

  • Equilibrium dialysis and pH titration determined binding stoichiometry and ligands.
  • NMR spectroscopy analyzed octarepeat structures.

    • Main Results:

    • Copper (Cu2+) specifically binds to SHaPrP(29-231), unlike other tested divalent cations.
    • Copper binding significantly alters PrP's tertiary structure, quenching fluorescence and shifting spectra.
    • Cu2+ binding promotes a conformational shift from alpha-helical to beta-sheet structures.
    • Binding stoichiometry is approximately 2 copper ions per PrP molecule.
    • Histidine residues within the octarepeat regions are implicated as key binding ligands.

    Conclusions:

    • Copper ions are specific ligands for the prion protein.
    • Copper binding induces significant structural changes in PrP, including a shift towards beta-sheet content.
    • The octarepeat regions of PrP are critical for copper binding.
    • These findings suggest a potential role for copper in the normal function of PrPC.