New advances in production and functional folding of G-protein-coupled receptors

被引:61
作者
Baneres, Jean-Louis [2 ,3 ,4 ]
Popot, Jean-Luc [5 ,6 ]
Mouillac, Bernard [1 ,3 ,4 ,7 ]
机构
[1] CNRS, UMR 5203, Inst Genom Fonct, Dept Mol Pharmacol, F-34000 Montpellier, France
[2] Fac Pharm Montpellier, CNRS, UMR 5247, Inst Biomol Max Mousseron, F-34000 Montpellier, France
[3] Univ Montpellier I, F-34000 Montpellier, France
[4] Univ Montpellier 2, F-34000 Montpellier, France
[5] CNRS, UMR 7099, Lab Phys Chim Mol Prot Membranaires, Inst Biol Phys Chim, F-75000 Paris, France
[6] Univ Paris 07, F-75000 Paris, France
[7] INSERM, U661, F-34000 Montpellier, France
关键词
MU-OPIOID-RECEPTOR; IN-VITRO; MEMBRANE-PROTEINS; AMPHIPATHIC POLYMERS; ELECTRON-MICROSCOPY; CRYSTAL-STRUCTURE; EXPRESSION; AMPHIPOLS; PURIFICATION; GPCR;
D O I
10.1016/j.tibtech.2011.03.002
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
G-protein-coupled receptors (GPCRs), the largest family of integral membrane proteins, participate in the regulation of many physiological functions and are the targets of approximately 30% of currently marketed drugs. However, knowledge of the structural and molecular bases of GPCR functions remains limited owing to difficulties related to their overexpression, purification and stabilization. The development of new strategies aimed at obtaining large amounts of functional GPCRs is therefore crucial. Here, we review the most recent advances in the production and functional folding of GPCRs from Escherichia coli inclusion bodies. Major breakthroughs open exciting perspectives for structural and dynamic investigations of GPCRs. In particular, combining targeting to bacterial inclusion bodies with amphipol-assisted folding is emerging as a highly powerful strategy.
引用
收藏
页码:314 / 322
页数:9
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