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Publication Abstract from PubMed

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.

Structure of a eukaryotic voltage-gated sodium channel at near-atomic resolution.,Shen H, Zhou Q, Pan X, Li Z, Wu J, Yan N Science. 2017 Mar 3;355(6328). pii: eaal4326. doi: 10.1126/science.aal4326. Epub , 2017 Feb 9. PMID:28183995^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.