{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Noland CL"],"funding":["Novo Nordisk Fonden"],"pagination":["1416"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8931054"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["Unlike classical voltage-gated sodium (Na<sub>V</sub>) channels, Na<sub>X</sub> has been characterized as a voltage-insensitive, tetrodotoxin-resistant, sodium (Na<sup>+</sup>)-activated channel involved in regulating Na<sup>+</sup> homeostasis. However, Na<sub>X</sub> remains refractory to functional characterization in traditional heterologous systems. Here, to gain insight into its atypical physiology, we determine structures of the human Na<sub>X</sub> channel in complex with the auxiliary β3-subunit. Na<sub>X</sub> reveals structural alterations within the selectivity filter, voltage sensor-like domains, and pore module. We do not identify an extracellular Na<sup>+</sup>-sensor or any evidence for a Na<sup>+</sup>-based activation mechanism in Na<sub>X</sub>. Instead, the S6-gate rema"],"journal":["Nature communications"],"pubmed_title":["Structure-guided unlocking of Na<sub>X</sub> reveals a non-selective tetrodotoxin-sensitive cation channel."],"pmcid":["PMC8931054"],"funding_grant_id":["NNF20OC0064550"],"pubmed_authors":["Tang J","Noland CL","Ciferri C","Kschonsak M","Pless SA","Heusser SA","Braun N","Chang T","Chua HC","Arthur CP","Payandeh J","Tam C"],"additional_accession":[]},"is_claimable":false,"name":"Structure-guided unlocking of Na<sub>X</sub> reveals a non-selective tetrodotoxin-sensitive cation channel.","description":"Unlike classical voltage-gated sodium (Na<sub>V</sub>) channels, Na<sub>X</sub> has been characterized as a voltage-insensitive, tetrodotoxin-resistant, sodium (Na<sup>+</sup>)-activated channel involved in regulating Na<sup>+</sup> homeostasis. However, Na<sub>X</sub> remains refractory to functional characterization in traditional heterologous systems. Here, to gain insight into its atypical physiology, we determine structures of the human Na<sub>X</sub> channel in complex with the auxiliary β3-subunit. Na<sub>X</sub> reveals structural alterations within the selectivity filter, voltage sensor-like domains, and pore module. We do not identify an extracellular Na<sup>+</sup>-sensor or any evidence for a Na<sup>+</sup>-based activation mechanism in Na<sub>X</sub>. Instead, the S6-gate rema","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Mar","modification":"2026-05-09T19:51:33.969Z","creation":"2025-02-19T00:56:42.487Z"},"accession":"S-EPMC8931054","cross_references":{"pubmed":["35301303"],"doi":["10.1038/s41467-022-28984-4"]}}