Copper Binding Extrinsic to the Octarepeat Region in the Prion Protein

Publisher: Bentham Science Publishers

E-ISSN: 1875-5550|10|5|529-535

ISSN: 1389-2037

Source: Current Protein and Peptide Science, Vol.10, Iss.5, 2009-10, pp. : 529-535

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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 PrP's 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.

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