ArticleEuropean biophysics journal : EBJ2017
Mutagenesis of the NaChBac sodium channel discloses a functional role for a conserved S6 asparagine.
Article in European biophysics journal : EBJ, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- The T1-tetramerisation domain of Kv1.2 rescues expression and preserves function of a truncated NaChBac sodium channel.FEBS letters · 2022Article
- Characterizing fenestration size in sodium channel subtypes and their accessibility to inhibitors.Biophysical journal · 2022Article
- An open state of a voltage-gated sodium channel involving a π-helix and conserved pore-facing asparagine.Biophysical journal · 2022Article
- Regulation and drug modulation of a voltage-gated sodium channel: Pivotal role of the S4-S5 linker in activation and slow inactivation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Batrachotoxin acts as a stent to hold open homotetrameric prokaryotic voltage-gated sodium channels.The Journal of general physiology · 2019Article
- A hypothetical molecular mechanism for TRPV1 activation that invokes rotation of an S6 asparagine.The Journal of general physiology · 2018Article
- CDtoolX, a downloadable software package for processing and analyses of circular dichroism spectroscopic data.Protein science : a publication of the Protein Society · 2018Article
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7 authors at 2 institutions in 2 countries.
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Abstract
Asparagine is conserved in the S6 transmembrane segments of all voltage-gated sodium, calcium, and TRP channels identified to date. A broad spectrum of channelopathies including cardiac arrhythmias, epilepsy, muscle diseases, and pain disorders is associated with its mutation. To investigate its effects on sodium channel functional properties, we mutated the simple prokaryotic sodium channel NaChBac. Electrophysiological characterization of the N225D mutant reveals that this conservative substitution shifts the voltage-dependence of inactivation by 25 mV to more hyperpolarized potentials. The mutant also displays greater thermostability, as determined by synchrotron radiation circular dichroism spectroscopy studies of purified channels. Based on our analyses of high-resolution structures of NaChBac homologues, we suggest that the side-chain amine group of asparagine 225 forms one or more hydrogen bonds with different channel elements and that these interactions are important for normal channel function. The N225D mutation eliminates these hydrogen bonds and the structural consequences involve an enhanced channel inactivation.
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