Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 276, Issue 20, Pages 16711-16719Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M006554200
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The prion protein is known to be a copper-binding protein, but affinity and stoichiometry data for the full-length protein at a physiological pH of 7 were lacking. Furthermore, it was unknown whether only the highly flexible N-terminal segment with its octarepeat region is involved in copper binding or whether the structured C-terminal domain is also involved, Therefore we systematically investigated the stoichiometry and affinity of copper binding to full-length prion protein PrP23-231 and to different N- and C-terminal fragments using electrospray ionization mass spectrometry and fluorescence spectroscopy. Our data indicate that the unstructured N-terminal segment is the cooperative copper-binding domain of the prion protein. The prion protein binds up to five copper(II) ions with half-maximal binding at similar to2 muM. This argues strongly for a direct role of the prion protein in copper metabolism, since it is almost saturated at about 5 muM, and the exchangeable copper Fool concentration in blood is about 8 muM.
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