ArticleThe journal of physical chemistry letters2023
Modulation of Pore Opening of Eukaryotic Sodium Channels by π-Helices in S6.
Article in The journal of physical chemistry letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 14 citations in OpenAlex.
- Lipid-based Nano-delivery systems as a promising strategy for the treatment of epilepsy: Current status and challenges.Epilepsia open · 2026Review
- AlphaFold2 captures conformational transitions in the voltage-gated channel superfamily.Biophysical journal · 2025Article
- π-Turns in Peptides: A Crystal-State Literature Survey.Journal of peptide science : an official publication of the European Peptide Society · 2025Review
- Calcium-activated chloride channel TMEM16A opens via pi-helical transition in transmembrane segment 4.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Impact of a Terahertz electromagnetic field on the ion permeation of potassium and sodium channels.Communications chemistry · 2025Article
- The chemistry of electrical signaling in sodium channels from bacteria and beyond.Cell chemical biology · 2024Review
- Unplugging lateral fenestrations of NALCN reveals a hidden drug binding site within the pore region.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Elucidating the clandestine behavior of enantiomeric DHPs in calcium channels.The Journal of general physiology · 2023Article
- Mechanisms of dihydropyridine agonists and antagonists in view of cryo-EM structures of calcium and sodium channels.The Journal of general physiology · 2023Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Voltage-gated sodium channels are heterotetrameric sodium selective ion channels that play a central role in electrical signaling in excitable cells. With recent advances in structural biology, structures of eukaryotic sodium channels have been captured in several distinct conformations corresponding to different functional states. The secondary structure of the pore lining S6 helices of subunits DI, DII, and DIV has been captured with both short π-helix stretches and in fully α-helical conformations. The relevance of these secondary structure elements for pore gating is not yet understood. Here, we propose that a π-helix in at least DI-S6, DIII-S6, and DIV-S6 results in a fully conductive state. On the other hand, the absence of π-helix in either DI-S6 or DIV-S6 yields a subconductance state, and its absence from both DI-S6 and DIV-S6 yields a nonconducting state. This work highlights the impact of the presence of a π-helix in the different S6 helices of an expanded pore on pore conductance, thus opening new doors toward reconstructing the entire conformational landscape along the functional cycle of Nav Channels and paving the way to the design of state-dependent modulators.
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