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Related Experiment Videos

Prion protein binds copper within the physiological concentration range.

M L Kramer1, H D Kratzin, B Schmidt

  • 1Department of Neuropathology, Georg August University of Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany. mkramer@med.uni-goettingen.de

The Journal of Biological Chemistry
|March 30, 2001
PubMed
Summary

The prion protein binds copper primarily through its flexible N-terminal region, with a high affinity suggesting a role in copper metabolism. This study clarifies copper binding stoichiometry and affinity for the full-length prion protein.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Metalloprotein research

Background:

  • The prion protein (PrP) is recognized as a copper-binding protein.
  • Limited data existed on the affinity and stoichiometry of copper binding to full-length PrP at physiological pH.
  • The specific domains of PrP involved in copper binding were not fully elucidated.

Purpose of the Study:

  • To systematically investigate the stoichiometry and affinity of copper binding to the full-length prion protein (PrP(23-231)).
  • To determine whether copper binding involves only the N-terminal segment or also the C-terminal domain.
  • To assess the role of PrP in copper metabolism based on binding characteristics.

Main Methods:

  • Electrospray ionization mass spectrometry (ESI-MS).

Related Experiment Videos

  • Fluorescence spectroscopy.
  • Investigation of full-length PrP(23-231) and various N- and C-terminal fragments.

    • Main Results:

    • The unstructured N-terminal segment acts as the cooperative copper-binding domain of the prion protein.
    • The prion protein binds up to five copper(II) ions.
    • Copper binding exhibits half-maximal saturation at approximately 2 micromolar (µM).

    Conclusions:

    • The N-terminal region of the prion protein is the primary site for copper binding.
    • High affinity and capacity for copper binding support a direct role for PrP in copper metabolism.
    • PrP is nearly saturated at physiological copper concentrations, highlighting its functional significance.