Abstract.
G protein-coupled receptors (GPCRS) represent a class of integral membrane proteins involved in many biological processes and pathologies. Fifty percent of all modern drugs and almost 25% of the top 200 bestselling drugs are estimated to target GPCRs. Despite these crucial biological implications, very little is known, at atomic resolution, about the detailed molecular mechanisms by which these membrane proteins are able to recognize their extra-cellular stimuli and transmit the associated messages. Obviously, our understanding of GPCR functioning would be greatly facilitated by the availability of high-resolution three-dimensional (3D) structural data. However, expression, solubilization and purification of these membrane proteins are not easy to achieve, and at present, only one 3D structure has been determined, that of bovine rhodopsin. This review presents and compares the different successful strategies which have been applied to solubilize and purify recombinant GPCRs in the perspective of structural biology experiments.
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29 June 2006
An Erratum to this paper has been published: https://doi.org/10.1007/s00018-006-0001-0
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Received 21 November 2005; received after revision 20 January 2006; accepted 2 February 2006
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Sarramegn, V., Muller, I., Milon, A. et al. Recombinant G protein-coupled receptors from expression to renaturation: a challenge towards structure. Cell. Mol. Life Sci. 63, 1149–1164 (2006). https://doi.org/10.1007/s00018-005-5557-6
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DOI: https://doi.org/10.1007/s00018-005-5557-6