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Copper Binding Extrinsic to the Octarepeat Region in the Prion Protein

[ Vol. 10 , Issue. 5 ]

Author(s):

Eric D. Walter, Daniel J. Stevens, Ann R. Spevacek, Micah P. Visconte, Andrew Dei Rossi and Glenn L. Millhauser   Pages 529 - 535 ( 7 )

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.

, Copper, Binding, Extrinsic, to, the, Octarepeat, Region, in, the, Prion, Protein

Affiliation:

Department of Chemistry&Biochemistry, University of California, Santa Cruz, Santa Cruz, CA 95064, USA.



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