Structure of a eukaryotic voltage-gated sodium channel at near-atomic resolution

Huaizong Shen, Qiang Zhou, Xiaojing Pan, Zhangqiang Li, Jianping Wu, Nieng Yan

Research output: Contribution to journalArticlepeer-review

314 Scopus citations


Voltage-gated sodium (Nav) 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 Nav channel from American cockroach (designated NavPaS) 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 VSDI, and a carboxy-terminal domain binds to the III-IV linker.The structure of NavPaS establishes an important foundation for understanding function and disease mechanism of Nav and related voltage-gated calcium channels.

Original languageEnglish (US)
Article numbereaal4326
Issue number6328
StatePublished - Mar 3 2017

All Science Journal Classification (ASJC) codes

  • General


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