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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...
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.
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 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...
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

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.
Sensory organs,...

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One-channel Cell-attached Patch-clamp Recording
13:07

One-channel Cell-attached Patch-clamp Recording

Published on: June 9, 2014

Gating in CNGA1 channels.

Monica Mazzolini1, Arin Marchesi, Alejandro Giorgetti

  • 1CBM S.c.r.l, Area Science Park SS 14 Km 163.5, 34012, Basovizza (TS), Trieste, Italy.

Pflugers Archiv : European Journal of Physiology
|November 10, 2009
PubMed
Summary
This summary is machine-generated.

Cyclic nucleotide-gated (CNG) and potassium (K+) channels share ancestry but differ functionally. This review explores their structural and functional divergence to elucidate CNG channel gating mechanisms.

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Ion Channel Physiology

Background:

  • Cyclic nucleotide-gated (CNG) and potassium (K+) channels exhibit significant amino acid sequence identity, suggesting a common evolutionary origin and similar 3D architecture.
  • Despite shared ancestry, CNG and K+ channels display markedly different physiological characteristics, including ion selectivity, voltage dependence, and desensitization properties.

Purpose of the Study:

  • To summarize and analyze the functional and structural distinctions between CNG and K+ channels.
  • To gain a deeper understanding of the gating mechanisms underlying CNG channel function.

Main Methods:

  • Comparative analysis of existing literature on CNG and K+ channel structure and function.
  • Review of experimental data and theoretical models related to ion channel gating.

Main Results:

  • K+ channels are characterized by high ionic selectivity, strong voltage-dependent gating, and inactivation upon sustained depolarization.
  • CNG channels exhibit low ion selectivity, minimal voltage dependence, and lack of desensitization in the presence of activating cyclic nucleotides.

Conclusions:

  • The profound functional differences between CNG and K+ channels highlight distinct evolutionary adaptations despite their shared ancestry.
  • Understanding these divergence points is crucial for deciphering the specific gating principles governing CNG channels.