Format

Send to

Choose Destination
Med Sci (Paris). 2012 Oct;28(10):837-44. doi: 10.1051/medsci/20122810011. Epub 2012 Oct 12.

[Handling G-protein-coupled receptors: expression, purification and in vitro stabilization].

[Article in French]

Author information

1
Institut des biomolécules Max Mousseron, faculté de pharmacie, Montpellier, France.

Abstract

Among the different classes of integral membrane proteins, G protein-coupled receptors (GPCR) constitute the largest family. They are involved in most essential physiological functions and particularly play a key role in cell-to-cell communication and sensory signal transduction. They represent targets for approximately 30% of currently marketed drugs. In order to better understand their functioning, define their tridimensional structure and develop novel selective and efficient therapeutic compounds, it is crucial to purify these proteins for a full characterization. However, this biochemical step is not trivial since GPCR are present in membranes at very low levels and they require detergents to be extracted from their natural lipid environment and be handled as functional proteins. No universal strategy for GPCR production, purification and stabilization is currently available; each single GPCR possesses a unique set of physicochemical characteristics, preference for some detergents upon solubilization and specific conditions for purification. During the last decade, major breakthroughs regarding overexpression, purification and above all GPCR stabilization, thanks to amphipols and nanodiscs, opened very exciting perspectives for structural and dynamic investigations of these membrane proteins. The aim of this chapter is to provide an overview of the different aspects of GPCR handling.

PMID:
23067414
DOI:
10.1051/medsci/20122810011
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for EDP Sciences
Loading ...
Support Center