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

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Title: Crystal structure of the human β2 adrenergic G-protein-coupled receptor.
Authors: Rasmussen, Søren G. F., Hee-Jung Choi, Rosenbaum, Daniel M., Kobilka, Tong Sun, Foon Sun Thian, Edwards, Patricia C., Burghammer, Manfred, Ratnala, Venkata R. P., Sanishvili, Ruslan, Fischetti, Robert F., Schertler, Gebhard F. X., Weis, William I., Kobilka, Brian K.
Source: Nature. 11/15/2007, Vol. 450 Issue 7168, p383-387. 5p. 4 Diagrams.
Subjects: Optical diffraction, Retina, Rhodopsin, Lattice theory, Neurotransmitters, Adrenergic receptors, Protoplasmic streaming, Polymer liquid crystals, Crystallography
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. [ABSTRACT FROM AUTHOR]
Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Crystal structure of the human β<subscript>2</subscript> adrenergic G-protein-coupled receptor.
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  Data: <searchLink fieldCode="DE" term="%22Optical+diffraction%22">Optical diffraction</searchLink><br /><searchLink fieldCode="DE" term="%22Retina%22">Retina</searchLink><br /><searchLink fieldCode="DE" term="%22Rhodopsin%22">Rhodopsin</searchLink><br /><searchLink fieldCode="DE" term="%22Lattice+theory%22">Lattice theory</searchLink><br /><searchLink fieldCode="DE" term="%22Neurotransmitters%22">Neurotransmitters</searchLink><br /><searchLink fieldCode="DE" term="%22Adrenergic+receptors%22">Adrenergic receptors</searchLink><br /><searchLink fieldCode="DE" term="%22Protoplasmic+streaming%22">Protoplasmic streaming</searchLink><br /><searchLink fieldCode="DE" term="%22Polymer+liquid+crystals%22">Polymer liquid crystals</searchLink><br /><searchLink fieldCode="DE" term="%22Crystallography%22">Crystallography</searchLink>
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  Data: 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. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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