SummaryVoltage-sensing domains (VSDs) undergo conformational changes in response to the membrane potential and are the critical structural modules responsible for the activation of voltage-gated channels. Structural information about the key conformational states underlying voltage activation is currently incomplete. Through the use of experimentally determined residue-residue interactions as structural constraints, we determine and refine a model of the Kv channel VSD in the resting conformation. The resulting structural model is in broad agreement with results that originate from various labs using different techniques, indicating the emergence of a consensus for the structural basis of voltage sensing
ABSTRACT: The voltage sensor domain (VSD) of voltage-gated cation (e.g., Na+, K+) channels central t...
The voltage sensor domain (VSD) of voltage-gated cation (e.g., Na(+), K(+)) channels central to neur...
Voltage-gated ion channels have a paramount importance in many physiological processes such as cell-...
SummaryVoltage-sensing domains (VSDs) undergo conformational changes in response to the membrane pot...
The voltage-sensing domain (VSD) is a common scaffold responsible for the transduction of transmembr...
The voltage sensor domain (VSD) is responsible for electromechanical transduction in voltage-gated i...
Voltage sensor domain (VSD) in channel and non-channel membrane proteins shares a common function in...
Voltage-gated ion channels open and close in response to changes in membrane potential, thereby enab...
Voltage-sensing domains (VSDs) couple changes in transmembrane electrical potential to conformationa...
Developing an understanding of the mechanism of voltage-gated ion channels in molecular terms requir...
Voltage sensor domains (VSDs) are structurally and functionally conserved protein modules that consi...
The voltage sensor domain (VSD) of voltage-gated cation (e.g., Na<sup>+</sup>, K<sup>+</sup>) channe...
SummaryA strong interplay between the voltage-sensor domain (VSD) and the pore domain (PD) underlies...
The mechanism of electromechanical transduction in voltage sensing domains remains controversial. He...
Voltage sensor domains (VSDs) regulate ion channels and enzymes by undergoing conformational changes...
ABSTRACT: The voltage sensor domain (VSD) of voltage-gated cation (e.g., Na+, K+) channels central t...
The voltage sensor domain (VSD) of voltage-gated cation (e.g., Na(+), K(+)) channels central to neur...
Voltage-gated ion channels have a paramount importance in many physiological processes such as cell-...
SummaryVoltage-sensing domains (VSDs) undergo conformational changes in response to the membrane pot...
The voltage-sensing domain (VSD) is a common scaffold responsible for the transduction of transmembr...
The voltage sensor domain (VSD) is responsible for electromechanical transduction in voltage-gated i...
Voltage sensor domain (VSD) in channel and non-channel membrane proteins shares a common function in...
Voltage-gated ion channels open and close in response to changes in membrane potential, thereby enab...
Voltage-sensing domains (VSDs) couple changes in transmembrane electrical potential to conformationa...
Developing an understanding of the mechanism of voltage-gated ion channels in molecular terms requir...
Voltage sensor domains (VSDs) are structurally and functionally conserved protein modules that consi...
The voltage sensor domain (VSD) of voltage-gated cation (e.g., Na<sup>+</sup>, K<sup>+</sup>) channe...
SummaryA strong interplay between the voltage-sensor domain (VSD) and the pore domain (PD) underlies...
The mechanism of electromechanical transduction in voltage sensing domains remains controversial. He...
Voltage sensor domains (VSDs) regulate ion channels and enzymes by undergoing conformational changes...
ABSTRACT: The voltage sensor domain (VSD) of voltage-gated cation (e.g., Na+, K+) channels central t...
The voltage sensor domain (VSD) of voltage-gated cation (e.g., Na(+), K(+)) channels central to neur...
Voltage-gated ion channels have a paramount importance in many physiological processes such as cell-...