Ligand-gated pentameric ion channels, from binding to gating

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

X-ray structures of molluscan acetylcholine-binding proteins and procaryotic proton-activated ion channels (ELIC and GLIC) enable us to model the ligand binding and activation mechanism of ligand-gated pentameric ion channels. Common versus distinct features can be deduced from the binding of agonists, antagonists and allosteric modulators in subunit interfaces of nicotinic acetylcholine, A-type γ-aminobutyric acid, glycine and 5-HT3-type serotonin receptors. Ligand interactions in subunit interfaces elicit conformational waves from the closure of the agonist-binding cavity through binding loops, ß-strands and transmembrane helices to pore gating.

Original languageEnglish
Pages (from-to)253-262
Number of pages10
JournalCurrent Molecular Pharmacology
Volume2
Issue number3
DOIs
Publication statusPublished - 2009

Fingerprint

Ligand-Gated Ion Channels
Acetylcholine
Ligands
Aminobutyrates
Receptors, Serotonin, 5-HT3
Ion Channels
Glycine
Protons
Carrier Proteins
X-Rays

Keywords

  • 5-HT
  • AChBP
  • Allostery
  • Binding-gating coupling
  • Cation-π and hydrogen bonding interactions
  • GABA
  • Glycine receptors
  • Homology modeling
  • Interface binding cavity
  • Nicotinic receptors
  • pLGIC
  • Receptors

ASJC Scopus subject areas

  • Drug Discovery
  • Pharmacology
  • Molecular Medicine

Cite this

Ligand-gated pentameric ion channels, from binding to gating. / Maksay, G.

In: Current Molecular Pharmacology, Vol. 2, No. 3, 2009, p. 253-262.

Research output: Contribution to journalArticle

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