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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...
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...
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...
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

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Local Anesthetics: Mechanism of Action01:23

Local Anesthetics: Mechanism of Action

Local anesthetics (LAs) block sensory and motor impulses by inhibiting the sodium channels on the nerve cell membranes. This induces temporary loss of sensation, relieving pain in a specific body area.
Local anesthetics are amphiphilic molecules consisting of a hydrophobic aromatic part linked to a hydrophilic group by an ester or amide linkage. They are weak bases and are usually available as salts, which increases their solubility and stability. Once administered, LAs exist in the body either...

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Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes
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Structural basis for the decrease in the outward potassium channel current induced by lanthanum.

Li Hong Wang1, Na Jiang, Bo Zhao

  • 1Jiangsu Key Laboratory of Biofunctional Materials, College of Chemistry and Environmental Science, Nanjing Normal University, Nanjing, 210046, People's Republic of China.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|July 27, 2010
PubMed
Summary

Lanthanum ions (La3+) reduce potassium (K+) channel activity in horseradish cells by directly binding to the K+ channel protein. This interaction disrupts the protein's structure and function, impacting ion transport.

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Area of Science:

  • Plant physiology
  • Biophysics
  • Computational chemistry

Background:

  • Potassium channels (K+ channels) are crucial for cellular function in plants and animals.
  • Understanding the interaction of metal ions with channel proteins is vital for biological and toxicological studies.

Purpose of the Study:

  • To investigate the effect of Lanthanum ions (La3+) on outward K+ channel current in horseradish.
  • To elucidate the direct interaction mechanism between La3+ and K+ channel proteins.

Main Methods:

  • Whole-cell patch-clamp technique to measure ion currents.
  • Molecular dynamics simulations to model ion-protein interactions.
  • Quantum chemistry calculations to analyze bonding.

Main Results:

  • La3+ was observed to decrease the outward K+ channel current in horseradish mesophyll cells.
  • Direct interaction involves the formation of coordination and hydrogen bonds between La3+ and the K+ channel protein.
  • This interaction leads to the destruction of the native protein structure, impairing channel function.

Conclusions:

  • La3+ directly inhibits K+ channel function in plants by altering protein structure.
  • Findings provide a theoretical basis for understanding high-valence metal ion interactions with channel proteins in various organisms.