Non-agonist-binding subunit interfaces confer distinct functional signatures to the alternate stoichiometries of the alpha4beta2 nicotinic receptor: an alpha4-alpha4 interface is required for Zn2+ potentiation.

Journal article

The alpha4beta2 subtype is the most abundant nicotinic acetylcholine receptor (nAChR) in the brain and possesses the high-affinity binding site for nicotine. The alpha4 and beta2 nAChR subunits assemble into two alternate stoichiometries, (alpha4)(2)(beta2)(3) and (alpha4)(3)(beta2)(2), which differ in their functional properties and sensitivity to chronic exposure to nicotine. Here, we investigated the sensitivity of both receptor stoichiometries to modulation by Zn2+. We show that Zn2+ exer...

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Authors: Moroni, M; Vijayan, R; Carbone, A; Zwart, R; Biggin, P

• Publication status: Published
• Journal: Journal of neuroscience : the official journal of the Society for Neuroscience
• Volume: 28
• Issue: 27
• Pages: 6884-6894
• Publication date: 2008-07-01
• DOI: 10.1523/jneurosci.1228-08.2008
• EISSN: 1529-2401
• ISSN: 0270-6474
• Language: English
• Keywords: Protein Binding; Xenopus laevis; Acetylcholine; Binding Sites; Oocytes; Amino Acid Substitution; Humans; Female; Synaptic Transmission; Amino Acid Sequence; Receptor Cross-Talk; Ligands; Membrane Potentials; Animals; Cell Membrane; Alanine; Protein Subunits; Receptors, Nicotinic; Models, Molecular; Receptor Aggregation; Zinc