Copper Binding to the N-Terminal Tandem Repeat Regions of Mammalian and Avian Prion Protein

New insights into cellular prion protein (PrPc) functions: The “ying and yang” of a relevant protein

“…By using synthetic peptides, several authors have reported that the OR region of PrP c binds Cu 2+ , and to a lesser extent Cu + , thereby modulating its intracellular levels (e.g., (Hornshaw et al, 1995a;Hornshaw et al, 1995b)). Indeed, synaptosomal fractions have revealed that the amount of copper in the brain of PrP c knockout mice is lower than in wild-type (WT) counterparts (Herms et al, 1999).…”

The yeast prion protein Ure2: Structure, function and folding

“…The relationship between domain structure and function for the PrP protein is more complex. The PrP protein has a flexible N-terminal tail [23,24] containing an octapeptide repeat region involved in copper binding [25], but this flexible region only partially overlaps with the segment that is required for infectivity (see Fig. 1).…”

“…The functional regions are as indicated. Repetitive regions correspond to Asn/Gln-rich regions, except for PrP, in which residues 60 to 91 include four copies of an octapeptide repeat sequence Pro-His-Gly-Gly-Gly-Trp-Gly-Gln (PHGGGWGQ) [25,118]. Fig.…”

Metal‐dependent α‐helix formation promoted by the glycine‐rich octapeptide region of prion protein

“…However, the octapeptide repeat is highly conserved among mammalian PrP c' proteins [14], implying some functional and structural roles of the octapeptide. A recent mass spectrometric study has shown that the octapeptide repeat provides a binding site for divalent metal ions, preferentially for Cu(II) [15]. The structure of a peptide consisting of four tandem repeats of the octapeptide has been investigated in the presence and absence of Cu(II) by using circular dichroism (CD) spectroscopy [16].…”