Crystal structure of the human β2 adrenergic G-protein-coupled receptor

Søren G. F. Rasmussen, Hee-Jung Choi, Daniel M. Rosenbaum, Tong Sun Kobilka, Foon Sun Thian, Patricia C. Edwards, Manfred Burghammer, Venkata R. P. Ratnala, Ruslan Sanishvili, Robert F. Fischetti, Gebhard F. X. Schertler, William I. Weis and Brian K. Kobilka ()
Additional contact information
Søren G. F. Rasmussen: Department of Molecular and Cellular Physiology and,
Hee-Jung Choi: Department of Molecular and Cellular Physiology and,
Daniel M. Rosenbaum: Department of Molecular and Cellular Physiology and,
Tong Sun Kobilka: Department of Molecular and Cellular Physiology and,
Foon Sun Thian: Department of Molecular and Cellular Physiology and,
Patricia C. Edwards: MRC Laboratory of Molecular Biology
Manfred Burghammer: European Synchrotron Radiation Facility, 6 rue Jules Horowitz, BP220, 38043 Grenoble, cedex 9, France
Venkata R. P. Ratnala: Department of Molecular and Cellular Physiology and,
Ruslan Sanishvili: Argonne National Laboratory, GM/CA-CAT, Boulevard 436, D007, 9700 South Cass Avenue, Argonne, Illinois 60439, USA
Robert F. Fischetti: Argonne National Laboratory, GM/CA-CAT, Boulevard 436, D007, 9700 South Cass Avenue, Argonne, Illinois 60439, USA
Gebhard F. X. Schertler: MRC Laboratory of Molecular Biology
William I. Weis: Department of Molecular and Cellular Physiology and,
Brian K. Kobilka: Department of Molecular and Cellular Physiology and,

Nature, 2007, vol. 450, issue 7168, 383-387

Abstract: Abstract Structural analysis of G-protein-coupled receptors (GPCRs) for hormones and neurotransmitters has been hindered by their low natural abundance, inherent structural flexibility, and instability in detergent solutions. Here we report a structure of the human β2 adrenoceptor (β2AR), which was crystallized in a lipid environment when bound to an inverse agonist and in complex with a Fab that binds to the third intracellular loop. Diffraction data were obtained by high-brilliance microcrystallography and the structure determined at 3.4 Å/3.7 Å resolution. The cytoplasmic ends of the β2AR transmembrane segments and the connecting loops are well resolved, whereas the extracellular regions of the β2AR are not seen. The β2AR structure differs from rhodopsin in having weaker interactions between the cytoplasmic ends of transmembrane (TM)3 and TM6, involving the conserved E/DRY sequences. These differences may be responsible for the relatively high basal activity and structural instability of the β2AR, and contribute to the challenges in obtaining diffraction-quality crystals of non-rhodopsin GPCRs.

Date: 2007
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DOI: 10.1038/nature06325

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