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• W1968830969 abstract "The prion protein (PrP) has been identified as a metalloprotein capable of binding multiple copper ions and possibly zinc. Recent studies now indicate that prion self-recognition may be an important factor in both the normal function and misfunction of this protein. We have developed fluorescently labeled models of the prion protein that allow prion−prion interactions and metal binding to be investigated on the molecular level. Peptides encompassing the full metal binding region were anchored to the surface of small unilamellar vesicles, and PrP−PrP interactions were monitored by fluorescence spectroscopy as a function of added metal. Both Cu2+ and Zn2+ were found to cause an increase in the level of PrP−PrP interactions, by 117 and 300%, respectively, whereas other metals such as Ni2+, Co2+, and Ca2+ had no effect. The binding of either of these cofactors appears to act as a switch that induces PrP−PrP interactions in a reversible manner. Both glutamine and tryptophan residues, which occur frequently in the metal binding region of PrP, were found to be important in mediating PrP−PrP interactions. Experiments demonstrate that tryptophan residues are also responsible for the low level of PrP−PrP interactions observed in the absence of Cu2+ and Zn2+, and this is further supported by molecular modeling. Overall, our results indicate that PrP may be a bifunctional molecule capable of responding to fluctuations in both neuronal Cu2+ and Zn2+ levels." @default.
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• W1968830969 date "2007-03-20" @default.
• W1968830969 modified "2023-10-04" @default.
• W1968830969 title "Copper and Zinc Promote Interactions between Membrane-Anchored Peptides of the Metal Binding Domain of the Prion Protein" @default.
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• W1968830969 doi "https://doi.org/10.1021/bi602473r" @default.
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