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-Structure paper
Title | Structure of a eukaryotic voltage-gated sodium channel at near-atomic resolution. |
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Journal, issue, pages | Science, Vol. 355, Issue 6328, Year 2017 |
Publish date | Mar 3, 2017 |
![]() | Huaizong Shen / Qiang Zhou / Xiaojing Pan / Zhangqiang Li / Jianping Wu / Nieng Yan / ![]() |
PubMed Abstract | 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 ...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. |
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Methods | EM (single particle) |
Resolution | 3.8 Å |
Structure data | |
Chemicals | ![]() ChemComp-NAG: |
Source |
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![]() | MEMBRANE PROTEIN / ion channel |