Copper Binding Extrinsic to the Octarepeat Region in the Prion Protein

Author(s): Eric D. Walter, Daniel J. Stevens, Ann R. Spevacek, Micah P. Visconte, Andrew Dei Rossi, Glenn L. Millhauser.

Journal Name: Current Protein & Peptide Science

Volume 10 , Issue 5 , 2009

Submit Manuscript
Submit Proposal

Abstract:

Current research suggests that the function of the prion protein (PrP) is linked to its ability to bind copper. PrP is implicated in copper regulation, copper buffering and copper-dependent signaling. Moreover, in the development of prion disease, copper may modulate the rate of protein misfolding. PrP possesses a number of copper sites, each with distinct chemical characteristics. Most studies thus far have concentrated on elucidating chemical features of the octarepeat region (residues 60-91, hamster sequence), which can take up to four equivalents of copper, depending on the ratio of Cu2+ to protein. However, other sites have been proposed, including those at histidines 96 and 111, which are adjacent to the octarepeats, and also at histidines within PrPs folded C-terminal domain. Here, we review the literature of these copper sites extrinsic to the octarepeat region and add new findings and insights from recent experiments.

Rights & PermissionsPrintExport Cite as


Article Details

VOLUME: 10
ISSUE: 5
Year: 2009
Page: [529 - 535]
Pages: 7
DOI: 10.2174/138920309789352056
Price: $58

Article Metrics

PDF: 2