Metal‐dependent α‐helix formation promoted by the glycine‐rich octapeptide region of prion protein

FEBS Letters

Hori-i, Ayako¹  Miura, Takashi¹  Takeuchi, Hideo¹ 

[1] Pharmaceutical Institute, Tohoku University, Aobayama, Sendai 980-77, Japan

关键词: Prion protein;    Secondary structure;    Metal coordination;    Raman spectroscopy;   

DOI  :  10.1016/0014-5793(96)01104-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Prion diseases share a common feature in that the normal cellular prion protein (PrP^C) converts to a proteaseresistant isoform PrP^Sc. The α-helix-rich C-terminal half of PrP^C is partly converted into β-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 α-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 α-helix formation.

【 授权许可】

Unknown