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Allosteric functioning of dimeric class C G-protein-coupled receptors.

Abstract : Whereas most membrane receptors are oligomeric entities, G-protein-coupled receptors have long been thought to function as monomers. Within the last 15 years, accumulating data have indicated that G-protein-coupled receptors can form dimers or even higher ordered oligomers, but the general functional significance of this phenomena is not yet clear. Among the large G-protein-coupled receptor family, class C receptors represent a well-recognized example of constitutive dimers, both subunits being linked, in most cases, by a disulfide bridge. In this review article, we show that class C G-protein-coupled receptors are multidomain proteins and highlight the importance of their dimerization for activation. We illustrate several consequences of this in terms of specific functional properties and drug development.
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Contributor : Angela Turner-Madeuf Connect in order to contact the contributor
Submitted on : Friday, September 15, 2006 - 10:49:31 AM
Last modification on : Monday, April 4, 2022 - 6:23:59 PM

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Jean-Philippe Pin, Julie Kniazeff, Jianfeng Liu, Virginie Binet, Cyril Goudet, et al.. Allosteric functioning of dimeric class C G-protein-coupled receptors.. FEBS Journal, Wiley, 2005, 272, pp.2947-55. ⟨10.1111/j.1742-4658.2005.04728.x⟩. ⟨inserm-00094959⟩



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