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- W2781981101 abstract "Abstract Cyclic nucleotide-gated (CNG) channels mediate transduction in several sensory neurons. These channels use the free energy of CNs’ binding to open the pore, a process referred to as gating. CNG channels belong to the superfamily of voltage-gated channels, where the motion of the α-helix S6 controls gating in most of its members. To date, only the open, cGMP-bound, structure of a CNG channel has been determined at atomic resolution, which is inadequate to determine the molecular events underlying gating. By using electrophysiology, site-directed mutagenesis, chemical modification, and Single Molecule Force Spectroscopy, we demonstrate that opening of CNGA1 channels is initiated by the formation of salt bridges between residues in the C-linker and S5 helix. These events trigger conformational changes of the α-helix S5, transmitted to the P-helix and leading to channel opening. Therefore, the superfamily of voltage-gated channels shares a similar molecular architecture but has evolved divergent gating mechanisms." @default.
- W2781981101 created "2018-01-12" @default.
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- W2781981101 date "2018-01-08" @default.
- W2781981101 modified "2023-10-01" @default.
- W2781981101 title "The gating mechanism in cyclic nucleotide-gated ion channels" @default.
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- W2781981101 doi "https://doi.org/10.1038/s41598-017-18499-0" @default.
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