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Allosteric Modulation of G Protein Coupled Receptors by Cytoplasmic, Transmembrane and Extracellular Ligands

Department of Structural Biology, School of Medicine, University of Pittsburgh, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA
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Pharmaceuticals 2010, 3(10), 3324-3342; https://doi.org/10.3390/ph3103324
Received: 9 August 2010 / Revised: 17 October 2010 / Accepted: 25 October 2010 / Published: 25 October 2010
(This article belongs to the Special Issue Allosteric Modulation)
G protein coupled receptors (GPCRs) bind diverse classes of ligands, and depending on the receptor, these may bind in their transmembrane or the extracellular domains, demonstrating the principal ability of GPCRs to bind ligand in either domains. Most recently, it was also observed that small molecule ligands can bind in the cytoplasmic domain, and modulate binding and response to extracellular or transmembrane ligands. Thus, all three domains in GPCRs are potential sites for allosteric ligands, and whether a ligand is allosteric or orthosteric depends on the receptor. Here, we will review the evidence supporting the presence of putative binding pockets in all three domains of GPCRs and discuss possible pathways of communication between these pockets. View Full-Text
Keywords: rhodopsin; metabotropic glutamate receptors; allosteric network; communication; membrane proteins rhodopsin; metabotropic glutamate receptors; allosteric network; communication; membrane proteins
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Yanamala, N.; Klein-Seetharaman, J. Allosteric Modulation of G Protein Coupled Receptors by Cytoplasmic, Transmembrane and Extracellular Ligands. Pharmaceuticals 2010, 3, 3324-3342.

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