6K41
cryo-EM structure of alpha2BAR-GoA complex
Summary for 6K41
Entry DOI | 10.2210/pdb6k41/pdb |
EMDB information | 9911 9912 |
Descriptor | Guanine nucleotide-binding protein G(o) subunit alpha, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, ... (6 entities in total) |
Functional Keywords | gpcr, complex, cryo-em, membrane protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 5 |
Total formula weight | 177619.78 |
Authors | Yuan, D.,Liu, Z.,Wang, H.W.,Kobilka, B.K. (deposition date: 2019-05-23, release date: 2020-04-15, Last modification date: 2020-05-13) |
Primary citation | Yuan, D.,Liu, Z.,Kaindl, J.,Maeda, S.,Zhao, J.,Sun, X.,Xu, J.,Gmeiner, P.,Wang, H.W.,Kobilka, B.K. Activation of the alpha2Badrenoceptor by the sedative sympatholytic dexmedetomidine. Nat.Chem.Biol., 16:507-512, 2020 Cited by PubMed Abstract: The α adrenergic receptors (αARs) are G protein-coupled receptors (GPCRs) that respond to adrenaline and noradrenaline and couple to the Gi/o family of G proteins. αARs play important roles in regulating the sympathetic nervous system. Dexmedetomidine is a highly selective αAR agonist used in post-operative patients as an anxiety-reducing, sedative medicine that decreases the requirement for opioids. As is typical for selective αAR agonists, dexmedetomidine consists of an imidazole ring and a substituted benzene moiety lacking polar groups, which is in contrast to βAR-selective agonists, which share an ethanolamine group and an aromatic system with polar, hydrogen-bonding substituents. To better understand the structural basis for the selectivity and efficacy of adrenergic agonists, we determined the structure of the αAR in complex with dexmedetomidine and Go at a resolution of 2.9 Å by single-particle cryo-EM. The structure reveals the mechanism of αAR-selective activation and provides insights into Gi/o coupling specificity. PubMed: 32152538DOI: 10.1038/s41589-020-0492-2 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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