Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2022 Jun 3;13:908867. doi: 10.3389/fphar.2022.908867

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2022 Jiang, Zhang and Xia.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

PMC Copyright notice

Topology and architecture of mammalian Na_V channels. (A) Topology of mammalian Na_V channels. D_I, D_II, D_III, IFM-motif and D_IV of α-subunit, β1 and β2 subunit are colored in cyan, red, green, purple, blue, brown and gray, respectively. A unique N-glycosylation site in Na_V1.5 and the cysteine residue for linking β2 are highlighted. P represents phosphorylation sites. (B) Subunits assembly of mammalian Na_V channels. A sugar moiety of N319 glycosylation and L869 block the binding of β1 and β2 to Na_V1.5 (PDB code: 6UZ3), respectively (Upper panels). Cryo-EM map of human Na_V1.7/β1/β2 (lower panel, EMDB code: EMD-33292). Dashed lines indicate the invisible region of β2 subunit. (C) Multiple ligand binding sites in mammalian Na_V channel α-subunit. Sodium ion and small-molecule modulators shown in spheres, polypeptide toxins shown in surface.