Article
Differential α4(+)/(-)β2 Agonist-binding Site Contributions to α4β2 Nicotinic Acetylcholine Receptor Function within and between Isoforms.
The Journal of biological chemistry - 29 Jan 2016
Lucero Linda M, Weltzin Maegan M, Eaton J Brek, Cooper John F, Lindstrom Jon M, Lukas Ronald J, Whiteaker Paul
Abstract excerpt
Two α4β2 nicotinic acetylcholine receptor (α4β2-nAChR) isoforms exist with (α4)2(β2)3 and (α4)3(β2)2 subunit stoichiometries and high versus low agonist sensitivities (HS and LS), respectively. Both isoforms contain a pair of α4(+)/(-)β2 agonist-binding sites. The LS isoform also contains a unique α4(+)/(-)α4 site with lower agonist affinity than the α4(+)/(-)β2 sites. However, the relative roles of the conserved...
Topics
- Acetylcholine
- Allosteric Site
- Animals
- Azetidines
- Binding Sites
- DNA, Complementary
- Electrophysiology
- Gene Expression Regulation
- Humans
- Mutagenesis, Site-Directed
- Mutation
- Nicotine
- Nicotinic Agonists