Transmission of extramembrane conformational change into current: Construction of metal-gated ion channel

Journal of the American Chemical Society

Volumn 128, Issue 18, 2006, Pages 6010-6011

  Kiwada, Tatsuto ^a   Sonomura, Kazuhiro ^a   Sugiura, Yukio ^a   Asami, Koji ^a   Futaki, Shiroh ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL; IRON; METAL;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHANNEL GATING; CHELATION; CONFORMATIONAL TRANSITION; PROTEIN CONFORMATION;

ALAMETHICIN; AMINO ACID SEQUENCE; CIRCULAR DICHROISM; ELECTROCHEMISTRY; FERRIC COMPOUNDS; ION CHANNEL GATING; ION CHANNELS; LEUCINE ZIPPERS; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTO-ONCOGENE PROTEINS C-FOS;

EID: 33646495755     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja060515b     Document Type: Article

References (21)

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17. The CD spectra of [Ida]Fos (the peptide corresponding to the extramembrane segment of Alm-[Ida]Fos) in the presence and absence of liposomes are almost identical with each other, suggesting that the [Ida]Fos segment has little interaction with the lipid membranes (Figure ID-ii).
18. 222 value of Alm-[Ida]Fos in the presence of liposomes is almost the sum of those for alamethicin in the membranes and for the [Ida]Fos peptide in the absence and presence of Fe(III). This suggests that the change in CD spectra of Alm-[Ida]Fos would mainly reflect the structural alternation of the extramembrane segment.
19. 8 a peptide having the same amino acid sequence as Alm-[Ida]Fos except that Ida at positions 42 and 44 are Ala and Gln, respectively (Supporting Information Figure S5).
20. Alm-Fos does not contain Ida residues, and the addition of Fe(III) caused no significant increase in the channel current levels (Supporting Information Figure S5).
21. Channel conductances of 0.08, 0.41, 1.44, and 1.88 nS were observed. These channel current levels are sometimes observed even in the absence of Fe(III) presumably due to the subtle difference in the assembly states or conformation of the peptide. and this difference may not be due to the interaction of Fe(III) with the channel pore.