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Related Concept Videos

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...
The Role of Ion Channels in Neuronal Computation01:19

The Role of Ion Channels in Neuronal Computation

A postsynaptic neuron usually receives numerous impulses from several other presynaptic neurons. The axon hillock of the postsynaptic neuron integrates all these signals and determines the likelihood of firing an action potential.
Sometimes a single EPSP is strong enough to induce an action potential in the postsynaptic neuron. However, multiple presynaptic inputs must often create EPSPs around the same time for the postsynaptic neuron to be sufficiently depolarized to fire an action potential.
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.
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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Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes
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Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes

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Small conductance calcium-activated potassium channels: from structure to function.

Kate L Weatherall1, Samuel J Goodchild, David E Jane

  • 1Departments of Physiology & Pharmacology, School of Medical Sciences, University of Bristol, University Walk, Bristol, UK.

Progress in Neurobiology
|April 3, 2010
PubMed
Summary
This summary is machine-generated.

Developing selective K(Ca)2 channel blockers is crucial for therapeutic applications. Structural modeling reveals apamin interacts with the outer pore of K(Ca)2.2 channels, not the selectivity filter, guiding future drug design.

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

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Related Experiment Videos

Last Updated: Jun 14, 2026

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes
10:19

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes

Published on: January 10, 2011

Determination of the Relative Cell Surface and Total Expression of Recombinant Ion Channels Using Flow Cytometry
11:32

Determination of the Relative Cell Surface and Total Expression of Recombinant Ion Channels Using Flow Cytometry

Published on: September 28, 2016

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

Area of Science:

  • Neuroscience
  • Pharmacology
  • Structural Biology

Background:

  • K(Ca)2 channels are crucial for neuronal excitability and have therapeutic potential for CNS disorders and arrhythmias.
  • Current K(Ca)2 channel blockers lack subtype selectivity, limiting their clinical utility.
  • Apamin, a bee venom toxin, exhibits partial selectivity for K(Ca)2 subtypes but has a narrow therapeutic window.

Purpose of the Study:

  • To structurally model the interaction of apamin with K(Ca)2.2 channels to understand selectivity.
  • To identify key regions involved in toxin-channel interactions for developing subtype-selective blockers.
  • To guide the design of novel K(Ca)2 channel modulators for therapeutic applications.

Main Methods:

  • Utilized mutational studies to identify key residues in K(Ca)2 channel block by apamin.
  • Employed molecular modeling by mapping K(Ca)2 channel sequences onto known ion channel crystal structures (KcsA, MthK, Kv1.2).
  • Performed structural modeling of apamin-K(Ca)2.2 interaction superimposed on the Kv1.2 crystal structure.

Main Results:

  • Mutagenesis studies highlighted the outer pore and S3-S4 loop's importance for apamin block.
  • Structural modeling indicated that apamin interacts with the outer pore of K(Ca)2.2 channels.
  • Apamin does not contact the K(Ca)2.2 channel's selectivity filter, explaining its limited selectivity.

Conclusions:

  • Understanding toxin- K(Ca)2 channel interactions is key to designing subtype-selective blockers.
  • Structural insights into apamin binding can inform the development of targeted therapeutics for conditions involving K(Ca)2 channels.
  • Comparative analysis of toxin interactions across K(Ca)2 subtypes will facilitate the creation of specific K(Ca)2 channel modulators.