hERG S4-S5 linker acts as a voltage-dependent ligand that binds to the activation gate and locks it in a closed state
Abstract Delayed-rectifier potassium channels (hERG and KCNQ1) play a major role in cardiac repolarization. These channels are formed by a tetrameric pore (S5–S6) surrounded by four voltage sensor domains (S1-S4). Coupling between voltage sensor domains and the pore activation gate is critical for c...
Saved in:
Main Authors: | Olfat A. Malak, Zeineb Es-Salah-Lamoureux, Gildas Loussouarn |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2017
|
Subjects: | |
Online Access: | https://doaj.org/article/fb63c05f0749402ab82a3705894795ad |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Up-regulation of voltage-gated sodium channels by peptides mimicking S4-S5 linkers reveals a variation of the ligand-receptor mechanism
by: Olfat A. Malak, et al.
Published: (2020) -
A standardised hERG phenotyping pipeline to evaluate KCNH2 genetic variant pathogenicity
by: Barbara Oliveira‐Mendes, et al.
Published: (2021) -
The S4-S5 linker acts as a signal integrator for HERG K+ channel activation and deactivation gating.
by: Chai Ann Ng, et al.
Published: (2012) -
Lipid regulation of hERG1 channel function
by: Williams E. Miranda, et al.
Published: (2021) -
Support Vector Machine model for hERG inhibitory activities based on the integrated hERG database using descriptor selection by NSGA-II
by: Keiji Ogura, et al.
Published: (2019)