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• W2088178594 endingPage "1059" @default.
• W2088178594 startingPage "1040" @default.
• W2088178594 abstract "The N-terminal region of the native human prion protein encompasses four highly conserved octarepeats that each contain a single His, Pro, Gln, and Trp residue as well as several Gly residues. At neutral pH these repeats are capable of individually binding copper (Cu(2+)) ions, involving the His side chain and the backbone amide of the Gly residues. In addition, the two His residues at positions 96 and 111 are also capable of binding Cu(2+). At low concentrations of the metal ion or at low pH, one Cu(2+) may be bound by multiple His residues of the four octarepeats. This complex is known to be redox active, while none of the other Cu(2+)-bound complexes are. Using density functional theory and molecular dynamics calculations data demonstrated how this form of the protein could reduce Cu(2+), through a process involving electron transfer from the Trp side chain. The reduced Cu gives rise to reactive oxygen species (ROS), which can lead to beta-cleavage of the prion protein chain at any of the Gly residues around position 90. Protein fragments of lengths similar to those arising from beta-cleavage are predominantly found in both healthy and Creutzfeldt-Jakob disease (CJD)-affected brains. Models of Cu binding to the His96 and His111 residues also indicate that different modes of Cu(2+) binding result in formation of stable beta-hairpin structures in this region of the protein. It is postulated that through interactions with the C-terminal part of the protein these hairpins may initiate misfolding and yield more stable beta-sheet structures that might associate in the same fashion with additional prion proteins." @default.
• W2088178594 created "2016-06-24" @default.
• W2088178594 creator A5001039339 @default.
• W2088178594 creator A5042190192 @default.
• W2088178594 date "2009-07-31" @default.
• W2088178594 modified "2023-10-13" @default.
• W2088178594 title "A Potential Mechanism for Cu²⁺Reduction, β-Cleavage, and β-Sheet Initiation Within The N-Terminal Domain of the Prion Protein: Insights from Density Functional Theory and Molecular Dynamics Calculations" @default.
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• W2088178594 doi "https://doi.org/10.1080/15287390903084389" @default.
• W2088178594 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19697239" @default.
• W2088178594 hasPublicationYear "2009" @default.
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