Neurotransmitter-gated ion channels as unconventional allosteric proteins
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2018, NeuropharmacologyMultiple binding sites in the nicotinic acetylcholine receptors: An opportunity for polypharmacolgy
2015, Pharmacological ResearchCitation Excerpt :Thus, it has been shown that the use of SBD, FBD and/or fishing strategies (alone or in combination) leads to promising results regarding the rational design of polypharmacological drugs [see for example [14,18,21–24]. Ligand-gated ion channels (LGICs) are defined as a group of transmembrane proteins which open when a ligand binds to an external region of the channel, allowing ions such as Na+, K+, Ca2+, or Cl− to pass through the membrane [25,26]. Members of the cys-loop LGIC family mediate both fast excitatory and inhibitory synaptic neurotransmission in the nervous system.
The nicotinic acetylcholine receptor and its prokaryotic homologues: Structure, conformational transitions & allosteric modulation
2015, NeuropharmacologyCitation Excerpt :Using AChBP as a structural model, conditions were found where ligands such as galanthamine, strychnine, cocaine, and morphine bind at micromolar concentrations (Hansen and Taylor, 2007; Nemecz and Taylor, 2011; Hamouda et al., 2013). Based on data collected on nAChR, the binding site of allosteric modulators that do not target the neurotransmitter site was initially suggested to be homologous to the benzodiazepines binding site in GABAA receptors (Galzi and Changeux, 1994). Although crystallographic evidence is still missing, considerable biochemical, pharmacological and modeling data support the notion that benzodiazepines allosterically potentiate GABAA receptors by binding to intersubunit sites in the EC domain that are homologous to the GABA sites but do not bind GABA (Smith and Olsen, 2000; Sawyer et al., 2002).
Allosteric ligands and their binding sites define γ-aminobutyric acid (gaba) type a receptor subtypes
2015, Advances in PharmacologyCitation Excerpt :The BZ binding site was shown to be located at the α +/γ- interface, as opposed to the GABA site at the β +/α- interface. The surprising observation was that the BZ binding sites were in the same homologous sequences (Loops A–H) as the GABA binding sites, which were the same utilized for agonist binding in all members of the cys-loop LGIC superfamily (Amin & Weiss, 1993; Duncalfe et al., 1996; Galzi & Changeux, 1994; Harrison & Lummis, 2006 Sawyer et al., 2002). This was immediately also recognized by workers on the GABAAR (Sigel & Buhr, 1997; Smith & Olsen, 1995) and indicated that the BZ sites were modified GABA agonist sites and these exogenous/ synthetic PAM ligands fortuitously found a site that was almost but not quite an agonist site!