Metal-dependent alpha-helix formation promoted by the glycine-rich octapeptide region of prion protein.

Miura T; Hori-i A; Takeuchi H

doi:10.1016/0014-5793(96)01104-0

Abstract

Prion diseases share a common feature in that the normal cellular prion protein (PrP(C)) converts to a protease-resistant isoform PrP(Sc). The alpha-helix-rich C-terminal half of PrP(C) is partly converted into beta-sheet in PrP(Sc). We have examined by Raman spectroscopy the structure of an octapeptide PHGGGWGQ that appears in the N-terminal region of PrP(C) and a longer peptide containing the octapeptide region. The peptides do not assume any regular structure without divalent metal ions, whereas Cu(II) binding to the HGGG segment induces formation of alpha-helical structure on the C-terminal side of the peptide chain. The N-terminal octapeptide of prion protein may be a novel structural motif that acts as a promoter of alpha-helix formation.

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References

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Metal-dependent alpha-helix formation promoted by the glycine-rich octapeptide region of prion protein.

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Authors

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Abstract

Full text links

References

Scrapie prion protein contains a phosphatidylinositol glycolipid.

Molecular biology of prion diseases.

Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene.

Altered circadian activity rhythms and sleep in mice devoid of prion protein.

Human prion protein cDNA: molecular cloning, chromosomal mapping, and biological implications.

Purification and properties of the cellular and scrapie hamster prion proteins.

Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein.

Z. Huang J.-M. Gabriel M.A. Baldwin R. Fletterick S.B. Prusiner F.E. Cohen Proc. Natl. Acad. Sci. USA 91 1994 7139 7143

NMR structure of the mouse prion protein domain PrP(121-231).

Prion protein peptides induce alpha-helix to beta-sheet conformational transitions.

Citations & impact

Impact metrics

Citations of article over time

Alternative metrics

Article citations

From Research to Diagnostic Application of Raman Spectroscopy in Neurosciences: Past and Perspectives.

Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance.

Using NMR spectroscopy to investigate the role played by copper in prion diseases.

Substitutions of PrP N-terminal histidine residues modulate scrapie disease pathogenesis and incubation time in transgenic mice.

Prion fragment peptides are digested with membrane type matrix metalloproteinases and acquire enzyme resistance through Cu²⁺-binding.

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Search life-sciences literature (45,103,589 articles, preprints and more)

Metal-dependent alpha-helix formation promoted by the glycine-rich octapeptide region of prion protein.

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Z. Huang J.-M. Gabriel M.A. Baldwin R. Fletterick S.B. Prusiner F.E. Cohen Proc. Natl. Acad. Sci. USA 91 1994 7139 7143

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