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Structure paper

TitleStructure of a eukaryotic voltage-gated sodium channel at near-atomic resolution.
Journal, issue, pagesScience, Vol. 355, Issue 6328, Year 2017
Publish dateMar 3, 2017
AuthorsHuaizong Shen / Qiang Zhou / Xiaojing Pan / Zhangqiang Li / Jianping Wu / Nieng Yan /
PubMed AbstractVoltage-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.
External linksScience / PubMed:28183995
MethodsEM (single particle)
Resolution3.8 Å
Structure data

6698

5x0m

EMDB-6698, PDB-5x0m:
Structure of a eukaryotic voltage-gated sodium channel at near atomic resolution
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • periplaneta americana (American cockroach)
KeywordsMEMBRANE PROTEIN / ion channel

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