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Related Concept Videos

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...
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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...
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GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
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Updated: May 26, 2026

A Fluorescent Screening Assay for Identifying Modulators of GIRK Channels
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Published on: April 24, 2012

Cys-loop receptor channel blockers also block GLIC.

Mona Alqazzaz1, Andrew J Thompson, Kerry L Price

  • 1Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom.

Biophysical Journal
|January 3, 2012
PubMed
Summary
This summary is machine-generated.

Gloeobacter ligand-gated ion channel (GLIC) shares similarities with human Cys-loop receptors. Researchers found that compounds blocking human channels also inhibit GLIC, revealing a unique pharmacological profile for the bacterial channel.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Structural Biology

Background:

  • Gloeobacter ligand-gated ion channel (GLIC) is a bacterial homolog of vertebrate Cys-loop ligand-gated ion channels.
  • The pore-lining region of GLIC exhibits high sequence homology to related proteins, suggesting functional similarities.

Purpose of the Study:

  • To investigate the pharmacological similarity between GLIC and vertebrate Cys-loop receptors.
  • To identify compounds that block GLIC channels and determine their binding sites and potency.

Main Methods:

  • Electrophysiology was used to test a range of compounds known to block Cys-loop receptors on GLIC.
  • Molecular docking studies were performed to predict ligand binding sites within the GLIC pore.
  • Site-directed mutagenesis was employed to validate predicted binding interactions.

Main Results:

  • Several compounds that block Cys-loop receptors also inhibited GLIC, demonstrating overlapping pharmacology.
  • Lindane, a GABA(A) receptor antagonist, was the most potent inhibitor (IC₅₀ = 0.2 μM), with potential binding at the 9' or 0'/2' residues.
  • Picrotoxinin and rimantadine (IC₅₀ = 2.6 μM) interacted with 2'Thr residues, confirmed by mutagenesis studies showing reduced potency in a T2'S mutant.

Conclusions:

  • The GLIC pore exhibits significant pharmacological overlap with Cys-loop receptors.
  • Despite similarities, GLIC possesses a distinct and unique pharmacology compared to its vertebrate counterparts.
  • These findings contribute to understanding ion channel function and developing targeted therapeutics.