@article{168081,
  keywords = {Animals, Conserved Sequence, Cryoelectron Microscopy, Glycosylation, Models, Chemical, Protein Domains, Periplaneta, voltage-gated sodium channels, Large-Conductance Calcium-Activated Potassium Channel alpha Subunits},
  author = {Huaizong Shen and Qiang Zhou and Xiaojing Pan and Zhangqiang Li and Jianping Wu and Nieng Yan},
  title = {Structure of a eukaryotic voltage-gated sodium channel at near-atomic resolution},
  abstract = {<p>Voltage-gated sodium (Na) channels are responsible for the initiation and propagation of action potentials. They are associated with a variety of channelopathies and are targeted by multiple pharmaceutical drugs and natural toxins. Here, we report the cryogenic electron microscopy structure of a putative Na channel from American cockroach (designated NaPaS) at 3.8 angstrom resolution. The voltage-sensing domains (VSDs) of the four repeats exhibit distinct conformations. The entrance to the asymmetric selectivity filter vestibule is guarded by heavily glycosylated and disulfide bond-stabilized extracellular loops. On the cytoplasmic side, a conserved amino-terminal domain is placed below VSD, and a carboxy-terminal domain binds to the III-IV linker. The structure of NaPaS establishes an important foundation for understanding function and disease mechanism of Na and related voltage-gated calcium channels.</p>
},
  year = {2017},
  journal = {Science},
  volume = {355},
  month = {03/2017},
  issn = {1095-9203},
  doi = {10.1126/science.aal4326},
  language = {eng},
}