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Related Concept Videos

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...
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...
Non-gated Ion Channels01:24

Non-gated Ion Channels

Ion channels are specialized proteins on the plasma membrane that allow charged ions to pass down their electrochemical gradient. Their main function is to maintain the membrane potential which is critical for cell viability. These channels are either gated or non-gated and can transport more than a thousand ions within milliseconds for the cellular event to occur.
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism.
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...
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...
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...

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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

Structural rearrangements underlying K+-channel activation gating.

E Perozo1, D M Cortes, L G Cuello

  • 1Department of Molecular Physiology and Biological Physics and Center for Structural Biology, University of Virginia Health Sciences Center, Charlottesville, VA 22906-0011, USA. eperozo@virginia.edu

Science (New York, N.Y.)
|July 3, 1999
PubMed
Summary

Researchers studied Streptomyces K+ channel gating using spin-labeling and EPR spectroscopy. They found rigid-body movements of transmembrane helices TM1 and TM2 open the ion channel pore.

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Area of Science:

  • Molecular biology
  • Biophysics
  • Structural biology

Background:

  • Potassium (K+) channels are crucial for cellular function.
  • Understanding K+ channel gating mechanisms is vital for pharmacology and physiology.
  • The Streptomyces K+ channel serves as a model system for studying ion channel activation.

Purpose of the Study:

  • To elucidate the intramembrane molecular events during activation gating of the Streptomyces K+ channel.
  • To characterize the conformational changes in transmembrane helices TM1 and TM2.
  • To investigate the role of specific residues in the gating mechanism.

Main Methods:

  • Site-directed spin-labeling (SDSL) techniques.
  • Electron paramagnetic resonance (EPR) spectroscopy.
  • Comparison of closed and open channel conformations.

Main Results:

  • Observed periodic changes in spin-label mobility and intersubunit spin-spin interactions.
  • Identified rigid-body movements, including translations and counterclockwise rotations, of TM1 and TM2 helices.
  • Demonstrated that TM2 movement expands the permeation pathway, leading to pore opening.
  • Noted immobility of extracellular residues near the selectivity filter but detected movements at the C-terminal pore helix.

Conclusions:

  • Activation gating involves coordinated rigid-body motion of transmembrane helices TM1 and TM2.
  • The TM2 helix plays a key role in pore dilation during channel opening.
  • Specific regions of the pore helix may be involved in transmitting gating signals.