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      Conformational complexity of G-protein-coupled receptors

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      Trends in Pharmacological Sciences

      Elsevier BV

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          Abstract

          G-protein-coupled receptors (GPCRs) are remarkably versatile signaling molecules. Members of this large family of membrane proteins respond to structurally diverse ligands and mediate most transmembrane signal transduction in response to hormones and neurotransmitters, and in response to the senses of sight, smell and taste. Individual GPCRs can signal through several G-protein subtypes and through G-protein-independent pathways, often in a ligand-specific manner. This functional plasticity can be attributed to structural flexibility of GPCRs and the ability of ligands to induce or to stabilize ligand-specific conformations. Here, we review what has been learned about the dynamic nature of the structure and mechanism of GPCR activation, primarily focusing on spectroscopic studies of purified human beta2 adrenergic receptor.

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          Author and article information

          Journal
          Trends in Pharmacological Sciences
          Trends in Pharmacological Sciences
          Elsevier BV
          01656147
          August 2007
          August 2007
          : 28
          : 8
          : 397-406
          Article
          10.1016/j.tips.2007.06.003
          17629961
          © 2007

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