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EMBO reports 9, 4, 363–369 (2008)
doi:10.1038/embor.2008.27
AOP Published online: 14 March 2008
Ligand sensitivity in dimeric associations of the serotonin 5HT2c receptor
EMBO Open
Filippo Mancia1, Zahra Assur1, Ariel G Herman1, Risa Siegel1 & Wayne A Hendrickson1, 2
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1 Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA
2 Howard Hughes Medical Institute, Columbia University, New York, New York 10032, USA
To whom correspondence should be addressed
Wayne A Hendrickson Tel: +1 212 305 3456; Fax: +1 212 305 7379; E-mail: wayne@convex.hhmi.columbia.edu
Received 5 June 2007; Accepted 22 January 2008; Published online 14 March 2008.
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Abstract
G-protein-coupled receptors (GPCRs) respond to external stimuli by activating heterotrimeric G proteins inside the cell. There is increasing evidence that many GPCRs exist as dimers or higher oligomers, but the biochemical nature of such dimers and what roles they have, if any, in signal transduction remains unclear. We conducted a comprehensive study of dimerization of the 5HT2c serotonin receptor using disulphide-trapping experiments. We found a dimer interface between transmembrane (TM) helices IV and V that is markedly sensitive to the state of receptor activation. This dimer seems to be quasisymmetrical in interfacial geometry and asymmetrical in its association with its cognate G protein. We also found a second interface at TM I helices, which is insensitive to the state of activation.
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