Résumé
Although expression of G protein-coupled receptors in heterologous systems such as yeast, insect, and mammal cells has proven to be highly useful for structural studies, bacterial systems have still an interest, in particular for specific purposes such as isotopic labeling in nuclear magnetic resonance analyses. Different approaches have been developed during the past years that consist in either expressing the receptor in bacterial membranes or in functional refolding from inclusion bodies. Here, we review the most recent advances in functional production and folding of GPCRs overexpressed in Escherichia coli and the subsequent stabilization of their native fold in solution.