Article
Mutations within the agonist-binding site convert the homomeric alpha1 glycine receptor into a Zn2+-activated chloride channel.
Channels (Austin, Tex.) - 1 Jan 2000
Grudzinska Joanna, Schumann Tanja, Schemm Rudolf, Betz Heinrich, Laube Bodo
Abstract excerpt
The divalent cation Zn2+ has been shown to regulate inhibitory neurotransmission in the mammalian CNS by affecting the activation of the strychnine-sensitive glycine receptor (GlyR). In spinal neurons and cells expressing recombinant GlyRs, low micromolar (<10 microM) concentrations of Zn2+ enhance glycine currents, whereas higher concentrations (>10 microM) have an inhibitory effect. Mutational studies have...
Topics
- Animals
- Binding Sites
- Biosensing Techniques
- Cations
- Chloride Channels
- Female
- Humans
- Ion Channels
- Ligands
- Mutation
- Oocytes
- Protein Structure, Tertiary
- Receptors, Glycine
- Xenopus laevis
- Zinc