Luciferase activity under direct ligand-dependent control of a muscarinic acetylcholine receptor.

ABSTRACT:

Background

Controlling enzyme activity by ligand binding to a regulatory domain of choice may have many applications e.g. as biosensors and as tools in regulating cellular functions. However, until now only a small number of ligand-binding domains have been successfully linked to enzyme activity. G protein-coupled receptors (GPCR) are capable of recognizing an extraordinary structural variety of extracellular signals including inorganic and organic molecules. Ligand binding to GPCR results in conformational changes involving the transmembrane helices. Here, we assessed whether ligand-induced conformational changes within the GPCR helix bundle can be utilized to control the activity of an integrated enzyme.

Results

As a proof of principle, we inserted the luciferase amino aci

SUBMITTER: Thor D 

PROVIDER: S-EPMC2689208 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature