@article{168061,
  keywords = {Animals, Models, Molecular, Amino Acid Sequence, Sequence Alignment, Cryoelectron Microscopy, Protein Domains, voltage-gated sodium channels, Electrophorus, Fish Proteins},
  author = {Zhen Yan and Qiang Zhou and Lin Wang and Jianping Wu and Yanyu Zhao and Gaoxingyu Huang and Wei Peng and Huaizong Shen and Jianlin Lei and Nieng Yan},
  title = {Structure of the Na1.4-β1 Complex from Electric Eel},
  abstract = {<p>Voltage-gated sodium (Na) channels initiate and propagate action potentials. Here, we present the cryo-EM structure of EeNa1.4, the Na channel from electric eel, in complex with the β1 subunit at 4.0\&nbsp;{\r A} resolution. The immunoglobulin domain of β1 docks onto the extracellular L5 and L6 loops of EeNa1.4 via extensive polar interactions, and the single transmembrane helix interacts with the third voltage-sensing domain (VSD). The VSDs exhibit "up" conformations, while the intracellular gate of the pore domain is kept open by a digitonin-like molecule. Structural comparison with closed NaPaS shows that the outward transfer of gating charges is coupled to the iris-like pore domain dilation through intricate force transmissions involving multiple channel segments. The IFM fast inactivation motif on the III-IV linker is plugged into the corner enclosed by the outer S4-S5 and inner S6 segments in repeats III and IV, suggesting a potential allosteric blocking mechanism for fast inactivation.</p>
},
  year = {2017},
  journal = {Cell},
  volume = {170},
  pages = {470-482.e11},
  month = {07/2017},
  issn = {1097-4172},
  doi = {10.1016/j.cell.2017.06.039},
  language = {eng},
}