Article
Additional acetylcholine (ACh) binding site at alpha4/alpha4 interface of (alpha4beta2)2alpha4 nicotinic receptor influences agonist sensitivity.
The Journal of biological chemistry - 2 Sept 2011
Mazzaferro Simone, Benallegue Naïl, Carbone Anna, Gasparri Federica, Vijayan Ranjit, Biggin Philip C, Moroni Mirko, Bermudez Isabel
Abstract excerpt
Nicotinic acetylcholine receptor (nAChR) α4 and β2 subunits assemble in two alternate stoichiometries to produce (α4β2)(2)α4 and (α4β2)(2)β2, which display different agonist sensitivities. Functionally relevant agonist binding sites are thought to be located at α4(+)/β2(-) subunit interfaces, but because these interfaces are present in both receptor isoforms, it is unlikely that they account for differences in...
Topics
- Acetylcholine
- Animals
- Binding Sites
- Cross-Linking Reagents
- Cysteine
- Electrophysiology
- Humans
- Ions
- Mutagenesis
- Mutation
- Oocytes
- Protein Conformation
- Protein Engineering