| http://purl.uniprot.org/citations/18042548 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18042548 | http://www.w3.org/2000/01/rdf-schema#comment | "The prion protein (PrP) is a cell-surface Cu(2+)-binding glycoprotein that when misfolded is responsible for a number of transmissible spongiform encephalopathies. Full-length PrP-(23-231) and constructs in which the octarepeat region has been removed, or His(95) and His(110) is replaced by alanine residues, have been used to elucidate the order and mode of Cu(2+) coordination to PrP-(23-231). We have built on our understanding of the appearance of visible CD spectra and EPR for various PrP fragments to characterize Cu(2+) coordination to full-length PrP. At physiological pH, Cu(2+) initially binds to full-length PrP in the amyloidogenic region between the octarepeats and the structured domain at His(95) and His(110). Only subsequent Cu(2+) ions bind to single histidine residues within the octarepeat region. Ni(2+) ions are used to further probe metal binding and, like Cu(2+), Ni(2+) will bind individually to His(95) and His(110), involving preceding main chain amides. Competitive chelators are used to determine the affinity of the first mole equivalent of Cu(2+) bound to full-length PrP; this approach places the affinity in the nanomolar range. The affinity and number of Cu(2+) binding sites support the suggestion that PrP could act as a sacrificial quencher of free radicals generated by copper redox cycling."xsd:string |
| http://purl.uniprot.org/citations/18042548 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m708472200"xsd:string |
| http://purl.uniprot.org/citations/18042548 | http://purl.uniprot.org/core/author | "Davies P."xsd:string |
| http://purl.uniprot.org/citations/18042548 | http://purl.uniprot.org/core/author | "Brown D.R."xsd:string |
| http://purl.uniprot.org/citations/18042548 | http://purl.uniprot.org/core/author | "Bowen S."xsd:string |
| http://purl.uniprot.org/citations/18042548 | http://purl.uniprot.org/core/author | "Viles J.H."xsd:string |
| http://purl.uniprot.org/citations/18042548 | http://purl.uniprot.org/core/author | "Klewpatinond M."xsd:string |
| http://purl.uniprot.org/citations/18042548 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18042548 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/18042548 | http://purl.uniprot.org/core/pages | "1870-1881"xsd:string |
| http://purl.uniprot.org/citations/18042548 | http://purl.uniprot.org/core/title | "Deconvoluting the Cu2+ binding modes of full-length prion protein."xsd:string |
| http://purl.uniprot.org/citations/18042548 | http://purl.uniprot.org/core/volume | "283"xsd:string |
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