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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.
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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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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
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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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Luminescence, the emission of light by a substance that has absorbed energy, is a process that involves the interaction of molecules with light. The energy-level diagram, or Jablonski diagram, is a graphical representation of these interactions, illustrating the various states and transitions a molecule can undergo. In a typical Jablonski diagram, the lowest horizontal line represents the ground-state energy of the molecule, which is usually a singlet state. This state represents the energies...
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Related Experiment Video

Updated: Jun 29, 2026

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development
09:32

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Published on: June 15, 2017

Domain movement in gelsolin: a calcium-activated switch.

R C Robinson1, M Mejillano, V P Le

  • 1Structural Biology Laboratory, Salk Institute for Biological Studies, Post Office Box 85800, San Diego, CA 92186-5800, USA.

Science (New York, N.Y.)
|December 3, 1999
PubMed
Summary
This summary is machine-generated.

The actin-binding protein gelsolin

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Published on: December 1, 2021

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Gelsolin is an actin-binding protein crucial for regulating the actin cytoskeleton.
  • It plays key roles in cellular processes like signaling, apoptosis, and movement.
  • Gelsolin's function involves severing and capping actin filaments, a process regulated by calcium ions.

Purpose of the Study:

  • To elucidate the structural basis of calcium-mediated gelsolin activation.
  • To understand how gelsolin remodels the actin cytoskeleton at a molecular level.

Main Methods:

  • X-ray crystallography was used to determine the 3.4 angstrom structure of the carboxyl-terminal half of gelsolin (domains G4-G6) bound to actin.
  • Structural analysis focused on the conformational changes induced by calcium binding.

Main Results:

  • Calcium binding triggers a significant conformational rearrangement in gelsolin.
  • Domain G6 undergoes a large flip and translation relative to domains G4 and G5.
  • This reorganization disrupts the beta sheet core of G4 and G6, exposing the actin-binding site.

Conclusions:

  • The revealed structure explains the mechanism of gelsolin activation by calcium.
  • The conformational changes directly enable gelsolin's actin-severing and capping activities.
  • Understanding gelsolin's structural dynamics provides insights into actin cytoskeleton regulation.