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• W2095353034 startingPage "463" @default.
• W2095353034 abstract "The characteristic gating properties of the HERG [human eag (ether-a-go-go)-related gene] potassium channel determine its contribution to cardiac repolarization and in setting the electrical behaviour of a variety of cells. In the present study we analysed, using a site-directed cysteine and disulfide chemistry approach, whether the eag/PAS (Per/Arnt/Sim) and proximal domains at the HERG N-terminus exert a role in controlling the access of the N-terminal flexible tail to its binding site in the channel core for interaction with the gating machinery. Whereas the eag/PAS domain is necessary for disulfide bridging, plus the cysteine residues introduced at positions 3 and 542 of the HERG sequence, the presence of the proximal domain seems to be dispensable. The state-dependent formation of a disulfide bridge between Cys3 and an endogenous cysteine residue at position 723 in the C-terminal C-linker suggests that the N-terminal tail of HERG can also get into close proximity with the C-linker structures located at the bottom of helix S6. Therefore the intrinsic flexibility of the N-tail and its proximity to both the S4-S5 loop and the C-linker may dynamically contribute to the modulation of HERG channel gating." @default.
• W2095353034 created "2016-06-24" @default.
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• W2095353034 date "2013-04-12" @default.
• W2095353034 modified "2023-10-06" @default.
• W2095353034 title "Mapping of interactions between the N- and C-termini and the channel core in HERG K+ channels" @default.
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• W2095353034 doi "https://doi.org/10.1042/bj20121717" @default.
• W2095353034 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23418776" @default.
• W2095353034 hasPublicationYear "2013" @default.
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