NR AILK
AU Miura,T.; Hori-i,A.; Takeuchi,H.
TI Metal-dependent alpha-helix formation promoted by the glycine-rich octapeptide region of prion protein
QU FEBS Letters 1996 Nov 4; 396(2-3): 248-52
PT journal article
AB Prion diseases share a common feature in that the normal cellular prion protein (PrPc) converts to a protease-resistant isoform PrPsc. The alpha-helix-rich C-terminal half of PrPc is partly converted into beta-sheet in PrPsc. We have examined by Raman spectroscopy the structure of an octapeptide PHGGGWGQ that appears in the N-terminal region of PrPc 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.
MH Amino Acid Sequence; Binding Sites; Copper/*metabolism; Glycine/analysis; Human; Molecular Sequence Data; Peptide Fragments/*chemistry/metabolism; PrPc Proteins/*chemistry/metabolism; *Protein Structure, Secondary; Spectrum Analysis, Raman; Support, Non-U.S. Gov't
AD Pharmaceutical Institute, Tohoku University, Sendai, Japan.
SP englisch
PO Niederlande