Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Extended lactation in high-yielding dairy cows. I. Effects on reproductive measurements.

Journal of dairy science·2018
Same author

Somatostatin-based radiopeptide therapy with [177Lu-DOTA]-TOC versus [90Y-DOTA]-TOC in neuroendocrine tumours.

European journal of nuclear medicine and molecular imaging·2013
Same author

High prevalence of genetically diverse Borrelia bavariensis-like strains in Ixodes persulcatus from Selenge Aimag, Mongolia.

Ticks and tick-borne diseases·2012
Same author

Dermal application of nitric oxide in vivo: kinetics, biological responses, and therapeutic potential in humans.

Clinical pharmacology and therapeutics·2012
Same author

[What is your diagnosis? Pruritic brown papules. Early secondary stage syphilis].

Der Hautarzt; Zeitschrift fur Dermatologie, Venerologie, und verwandte Gebiete·2008
Same author

[Cytokine-based and targeted therapy of metastatic renal cell carcinoma--a current analysis].

Aktuelle Urologie·2007

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.

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.