FEBS Letters | |
Metal‐dependent α‐helix formation promoted by the glycine‐rich octapeptide region of prion protein | |
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 (PrPC) converts to a proteaseresistant isoform PrPSc. The α-helix-rich C-terminal half of PrPC is partly converted into β-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 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
【 预 览 】
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RO201912020303461ZK.pdf | 423KB | download |