Logo Université de Strasbourg


Sur ce site

Sur le Web du CNRS

Accueil > UMR 7242 Biotechnologie et signalisation cellulaire (Jean-Luc Galzi) > Récepteurs, protéines membranaires et innovation thérapeutique (Animation scientifique : Isabelle Schalk) > RCPG, douleur et inflammation (Frédéric Simonin) > Nos thématiques > GPCRs and associated proteins

GPCRs and associated proteins

Structural and functional studies on purified GPCRs and interacting partners

The availability of milligram amounts of active purified GPCRs opens the way to study their behaviour at the molecular level in different model environments, including the dynamics of their interaction with specific protein partners. Such purified material offers additional opportunities to develop a panel of downstream applications such as antibody production, protein array construction, functional assays or ligand screening. Ultimately, obtaining cristallization-grade purified receptors is highly desired to get access to their 3D structure and to eventually develop structure-based drug discovery. Producing and recovering the required amounts of active, pure and homogenous GPCRs is however still highly challenging as it results from a fastidious combination between efficient and reliable bioproduction systems, accurate extraction and purification procedures and tailor-made stabilization strategies.

3D structural information is today available for only 6 class A GPCRs (Congreve et al. 2011), as compared to the circa 800 identified GPCRs in human. The success rate is quite always receptor-dependent so that these activities are mainly coped on a case-by-case basis and generic methods are still to be developed.

Capitalizing on the expertise we gained in the past on the development of dedicated methods and tools for the production, purification and analysis of recombinant GPCRs (Singh et al. 2008 ; Alkhalfioui et al. 2009 ; Magnin et al. 2009 ; Michalke et al. 2009 ; Ferndahl et al. 2010 ; Michalke et al. 2010), our goal will be to retrieve structural and functional data from biochemical and biophysical studies on the proteins of interest for the laboratory (see project 1, 2 and 3).


References :

Singh et al, 2008, Microb. Cell. Fact. 7, 28

Alkhalfioui et al, 2009, Curr Opin Pharmacol 9, 629-635

Magnin et al, 2009, Protein Expr. Purif. 64, 1-7

Michalke et al, 2009, Anal Biochem 386, 147-155

Ferndahl et al, 2010, Microb Cell Fact 9, 47

Michalke et al, 2010, Anal Biochem 401, 74-80

Congreve et al, 2011, J. Med. Chem. 54, 4283-311

Bornert et al, 2012, Curr. Protoc. Protein Sci. Chapter 29:Unit 29.2


- Back to the team homepage