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Effects of an alpha-helical ryanodine receptor C-terminal tail peptide on ryanodine receptor activity: modulation by Homer

Pouliquin, Pierre; Pace, Suzy M; Curtis, Suzanne; Harvey, Peta; Gallant, Esther; Zorzato, Francesco; Casarotto, Marco; Dulhunty, Angela


We have determined the structure of a domain peptide corresponding to the extreme 19 C-terminal residues of the ryanodine receptor Ca2+ release channel. We examined functional interactions between the peptide and the channel, in the absence and in the presence of the regulatory protein Homer. The peptide was partly α-helical and structurally homologous to the C-terminal end of the T1 domain of voltage-gated K+ channels. The peptide (0.1-10 μM) inhibited skeletal ryanodine receptor channels when...[Show more]

CollectionsANU Research Publications
Date published: 2006
Type: Journal article
Source: The International Journal of Biochemistry and Cell Biology
DOI: 10.1016/j.biocel.2006.03.020


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