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Residues that mediate helix–helix interactions within the seven transmem-branes (TM) of G protein-coupled receptors are important for receptor biogenesis and the receptor switch mechanism. By contrast, the residues directly contacting the lipid bilayer have only recently garnered attention as potential receptor dimerization interfaces. | Complement factor 5a receptor chimeras reveal the importance of lipid-facing residues in transport competence Jeffery M. Klco1 Saurabh Sen1 Jakob L. Hansen2 3 Christina Lyngs02 3 Gregory V. Nikiforovich4 Soren P. Sheikh5 and Thomas J. Baranski1 1 Departments of Medicine and Molecular Biology Pharmacology Washington University Schoolof Medicine St Louis MO USA 2 Laboratory for Molecular Cardiology Danish NationalResearch Foundation Centre for Cardiac Arrhythmia The Heart Centre Copenhagen University Hospital Denmark 3 Laboratory for Molecular Cardiology Danish NationalResearch Foundation Centre for Cardiac Arrhythmia Department of Neuroscience and Pharmacology University of Copenhagen Denmark 4 Department of Biochemistry and Molecular Biophysics Washington University Schoolof Medicine St Louis MO USA 5 The Laboratory of Molecular and Cellular Cardiology Department of Biochemistry Pharmacology and Genetics University Hospitalof Odense Denmark Keywords BRET C5aR G protein-coupled receptor lipid-facing transmembrane helix Correspondence T. J. Baranski Departments of Medicine and Molecular Biology Pharmacology Washington University Schoolof Medicine Campus Box 8127 660 South Euclid Avenue St Louis MO 63110 USA Fax 1 314 362 7641 Tel 1 314 747 3997 E-mail baranski@wustl.edu These authors contributed equally to this work Present addresses fNeurology CNET University of Alabama at Birmingham AL USA iMolLife Design LLC St Louis MO USA Received 14 January 2009 revised 3 March 2009 accepted 12 March 2009 doi 10.1111 j.1742-4658.2009.07002.x Residues that mediate helix-helix interactions within the seven transmembranes TM of G protein-coupled receptors are important for receptor biogenesis and the receptor switch mechanism. By contrast the residues directly contacting the lipid bilayer have only recently garnered attention as potential receptor dimerization interfaces. In the present study we aimed to determine the contributions of these lipid-facing residues to receptor .
