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A novel copper(II) coordination at His186 in full-length murine prion protein

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Title: A novel copper(II) coordination at His186 in full-length murine prion protein
Authors: Watanabe, Yasuko Browse this author
Hiraoka, Wakako Browse this author
Igarashi, Manabu Browse this author →KAKEN DB
Ito, Kimihito Browse this author →KAKEN DB
Shimoyama, Yuhei Browse this author
Horiuchi, Motohiro Browse this author →KAKEN DB
Yamamori, Tohru Browse this author →KAKEN DB
Yasui, Hironobu Browse this author →KAKEN DB
Kuwabara, Mikinori Browse this author
Inagaki, Fuyuhiko Browse this author →KAKEN DB
Inanami, Osamu Browse this author →KAKEN DB
Keywords: Prion protein
C-terminal domain
Interspin distance
Dipolar interaction
Histidine residue
Issue Date: 9-Apr-2010
Publisher: Elsevier
Journal Title: Biochemical and Biophysical Research Communications
Volume: 394
Issue: 3
Start Page: 522
End Page: 528
Publisher DOI: 10.1016/j.bbrc.2010.03.003
PMID: 20206606
Abstract: To explore Cu(II) ion coordination by His186 in the C-terminal domain of full-length prion protein (moPrP), we utilized the magnetic dipolar interaction between a paramagnetic metal, Cu(II) ion, and a spin probe introduced in the neighborhood of the postulated binding site by the spin labeling technique (SDSL technique). Six moPrP mutants, moPrP(D143C), moPrP(Y148C), moPrP(E151C), moPrP(Y156C), moPrP(T189C), and moPrP(Y156C,H186A), were reacted with a methane thiosulfonate spin probe and a nitroxide residue (R1) was created in the binding site of each one. Line broadening of the ESR spectra was induced in the presence of Cu(II) ions in moPrP(Y148R1), moPrP(Y151R1), moPrP(Y156R1), and moPrP( T189R1) but not moPrP(D143R1). This line broadening indicated the presence of electron–electron dipolar interaction between Cu(II) and the nitroxide spin probe, suggesting that each interspin distance was within 20 Å. The interspin distance ranges between Cu(II) and the spin probes of moPrP(Y148R1), moPrP(Y151R1), moPrP(Y156R1), and moPrP(T189R1) were estimated to be 12.1 Å, 18.1 Å, 10.7 Å, and 8.4 Å, respectively. In moPrP(Y156R1,H186A), line broadening between Cu(II) and the spin probe was not observed. These results suggest that a novel Cu(II) binding site is involved in His186 in the Helix2 region of the C-terminal domain of moPrPC.
Type: article (author version)
Appears in Collections:獣医学院・獣医学研究院 (Graduate School of Veterinary Medicine / Faculty of Veterinary Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 稲波 修

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