Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation

Guillaume Lebon, Tony Warne, Patricia C. Edwards, Kirstie Bennett, Christopher J. Langmead, Andrew G. W. Leslie and Christopher G. Tate ()
Additional contact information
Guillaume Lebon: MRC Laboratory of Molecular Biology, Hills Road
Tony Warne: MRC Laboratory of Molecular Biology, Hills Road
Patricia C. Edwards: MRC Laboratory of Molecular Biology, Hills Road
Kirstie Bennett: Heptares Therapeutics, BioPark, Broadwater Road
Christopher J. Langmead: Heptares Therapeutics, BioPark, Broadwater Road
Andrew G. W. Leslie: MRC Laboratory of Molecular Biology, Hills Road
Christopher G. Tate: MRC Laboratory of Molecular Biology, Hills Road

Nature, 2011, vol. 474, issue 7352, 521-525

Abstract: Adenosine A2A receptor structure Adenosine receptors are G protein-coupled receptors that are found in the heart and the brain, and adenosine is the endogenous ligand for this class of transmembrane receptor. Lebon et al. present two X-ray crystal structures of a thermostabilized human adenosine A2A receptor bound to its endogenous agonist adenosine and the synthetic agonist NECA. Comparison of the agonist-bound structures of A2A receptor with the agonist-bound structures of β-adrenoceptors suggests that the contraction of the ligand binding pocket caused by the inward motion of several helices may be a common feature in the activation of all G protein-coupled receptors.

Date: 2011
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DOI: 10.1038/nature10136

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