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lüll Copper binding extrinsic to the octarepeat region in the prion protein Walter ED; Stevens DJ; Spevacek AR; Visconte MP; Dei Rossi A; Millhauser GLCurr Protein Pept Sci 2009[Oct]; 10 (5): 529-35Current 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.|Amino Acid Sequence[MESH]|Animals[MESH]|Binding Sites[MESH]|Biochemistry/*methods[MESH]|Copper/*chemistry[MESH]|Histidine/chemistry[MESH]|Humans[MESH]|Molecular Sequence Data[MESH]|Prions/*chemistry[MESH]|Protein Binding[MESH]|Protein Denaturation[MESH]|Protein Folding[MESH]|Protein Structure, Tertiary[MESH]|Sequence Homology, Amino Acid[MESH]|Signal Transduction[MESH] |