Copper binding to the PrP isoforms: a putative marker of their conformation and function.
We show here that PrP(C), the normal isoform of the prion protein (PrP(Sc)), could be retained by a Cu(2+)-loaded resin through two different binding sites. Contrarily, PrP(Sc) was not retained at all by such resin. This constitutes a new prion-specific property of PrP(Sc), which in addition to protease resistance and beta-sheet content, may result from its aberrant conformation.
Shaked
Y
Y
Department of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital, Jerusalem, Israel.
Rosenmann
H
H
Hijazi
N
N
Halimi
M
M
Gabizon
R
R
D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods; D003300:Copper / Q000378:metabolism*; D006224:Cricetinae; D018621:PrPC Proteins / Q000737:chemistry* / Q000378:metabolism*; D018620:PrPSc Proteins / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D020033:Protein Isoforms / Q000378:metabolism
D018621:PrPC Proteins; D018620:PrPSc Proteins; D020033:Protein Isoforms; D003300:Copper