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Related Concept Videos

Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that include the...
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that include the...
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...

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Updated: Jun 26, 2026

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
15:28

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells

Published on: October 1, 2010

Model development for the viral Kcv potassium channel.

Sascha Tayefeh1, Thomas Kloss, Michael Kreim

  • 1Eduard Zintl-Institut für Anorganische und Physikalische Chemie, Technische Universität Darmstadt, Darmstadt, Germany.

Biophysical Journal
|January 27, 2009
PubMed
Summary

Researchers developed a computational model of the Kcv potassium channel

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Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies
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Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies

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Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies
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Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies

Published on: January 22, 2015

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Last Updated: Jun 26, 2026

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
15:28

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells

Published on: October 1, 2010

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies
10:22

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies

Published on: July 13, 2013

Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies
11:42

Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies

Published on: January 22, 2015

Area of Science:

  • Computational biology
  • Structural biology
  • Biophysics

Background:

  • The Kcv channel is a short viral potassium channel critical for ion transport.
  • Understanding the open state dynamics of ion channels is essential for pharmacology and disease research.
  • The N-terminal region and lysine residue protonation states are key factors influencing channel function.

Purpose of the Study:

  • To create and validate a computational model for the open state of the Kcv potassium channel.
  • To investigate ion permeation mechanisms and the role of flexible regions and charged residues.
  • To integrate diverse experimental and theoretical data for robust model development.

Main Methods:

  • Homology modeling was used to build the initial channel structure.
  • Extensive molecular-dynamics simulations were performed in a membrane environment.
  • Data from NMR spectroscopy, electrophysiology, and 3D reference interaction site model (RISM) integral equation theory were integrated.

Main Results:

  • The final model accurately reproduced spontaneous ion transitions across the Kcv channel pore.
  • Non-equilibrium transport events were simulated reproducibly without artificial ion placement or excessive driving potentials.
  • The ion transport mechanism through the filter region aligns with single-file motion, coupled to ion exchange with the cavity.

Conclusions:

  • The developed computational model provides a reliable representation of the Kcv channel's open state.
  • The study elucidates the mechanism of ion permeation, highlighting the interplay between the filter, cavity, and flexible N-terminal regions.
  • This model serves as a valuable tool for future studies on potassium channel function and modulation.