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- W2020306783 abstract "The prion protein (PrP) is implicated in the fatal neurodegenerative diseases known as transmissible spongiform encephalopathies (TSEs). These illnesses are unique because a cellular form of PrP misfolds to create an infectious agent, PrPSc. All birds and mammals produce PrP, however, very few naturally develop TSEs. Despite the fact that PrP is conserved among these species, little is known about its normal physiological function. Growing evidence suggests that PrP binds both copper and zinc in vivo. These metals induce PrP endocytosis, inhibit in vitro fibril formation, and promote intermolecular interactions. Metal binding occurs in the flexible and unstructured N-terminal half of PrP. Zinc binding is restricted to the repeat region known as the octarepeats (PHGGGWGQ), in which the four histidines from the octarepeat domain coordinate a single Zn2+ atom. The structured C-terminal domain is the proposed initiation site of the conversion to PrPSc. The global structure of PrP bound to Zn2+ is unknown, and in particular, whether metal ion coordination influences the structured C-terminal domain. To study the potential interaction of the N- and C- termini upon Zn2+ binding, we created 15N labeled mouse PrP for NMR studies. We titrated Zn2+ into the protein and examined the changes in the HSQC spectra. The results from this study will help to determine whether Zn2+ plays a protective or harmful role in the progression to prion diseases. Furthermore, it might lend insight into the physiological function of PrP." @default.
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- W2020306783 date "2010-01-01" @default.
- W2020306783 modified "2023-10-14" @default.
- W2020306783 title "The Influence of Zn2+ on the Global Structure of the Prion Protein" @default.
- W2020306783 doi "https://doi.org/10.1016/j.bpj.2009.12.4219" @default.
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