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 Mar 17;13:858348. doi: 10.3389/fphar.2022.858348

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

Copyright © 2022 Wisedchaisri and Gamal El-Din.

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

Druggability of the voltage sensor in the resting, deactivated, and inactivated states. (A,B) Structures of HwTx-IV (A) and ProTx-II (B) bound to the aqueous cleft of Na_VAb/human Na_V1.7-VSD2 chimera. Molecular surface of VSD2 is colored by electrostatic potentials (red—negative; blue—positive). Positively charged lysine and arginine residues of the toxins interact with negatively charged residues located in the S3-S4 hairpin. A tryptophan residue from the toxins provides additional van der Waals interaction with the receptor. (C) GX-936 aryl sulfonamide antagonist bound to the aqueous cleft of Na_VAb/human Na_V1.7-VSD4 chimera. Carbon atoms of GX-936 are colored in yellow. Residues from VSD4 forming the binding site are shown as sticks. The gating charge arginines R1-R4 are shown in blue.