The gating mechanism in cyclic nucleotide-gated ion channels.
In: Scientific reports, Jg. 8 (2018-01-08), Heft 1, S. 45
Online
academicJournal
Zugriff:
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.
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The gating mechanism in cyclic nucleotide-gated ion channels.
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Autor/in / Beteiligte Person: | Mazzolini, M ; Arcangeletti, M ; Marchesi, A ; Napolitano, LMR ; Grosa, D ; Maity, S ; Anselmi, C ; Torre, V |
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Zeitschrift: | Scientific reports, Jg. 8 (2018-01-08), Heft 1, S. 45 |
Veröffentlichung: | London : Nature Publishing Group, copyright 2011-, 2018 |
Medientyp: | academicJournal |
ISSN: | 2045-2322 (electronic) |
DOI: | 10.1038/s41598-017-18499-0 |
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