6K41

cryo-EM structure of alpha2BAR-GoA complex


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.90 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Activation of the alpha2Badrenoceptor by the sedative sympatholytic dexmedetomidine.

Yuan, D.Liu, Z.Kaindl, J.Maeda, S.Zhao, J.Sun, X.Xu, J.Gmeiner, P.Wang, H.W.Kobilka, B.K.

(2020) Nat Chem Biol 16: 507-512

  • DOI: https://doi.org/10.1038/s41589-020-0492-2
  • Primary Citation of Related Structures:  
    6K41, 6K42

  • PubMed Abstract: 

    The α 2 adrenergic receptors (α 2 ARs) are G protein-coupled receptors (GPCRs) that respond to adrenaline and noradrenaline and couple to the Gi/o family of G proteins. α 2 ARs play important roles in regulating the sympathetic nervous system. Dexmedetomidine is a highly selective α 2 AR 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 α 2B AR in complex with dexmedetomidine and Go at a resolution of 2.9 Å by single-particle cryo-EM. The structure reveals the mechanism of α 2 AR-selective activation and provides insights into Gi/o coupling specificity.


  • Organizational Affiliation

    Beijing Advanced Innovation Center for Structural Biology, Tsinghua University, Beijing, China.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Guanine nucleotide-binding protein G(o) subunit alpha354Homo sapiensMutation(s): 0 
Gene Names: GNAO1
Membrane Entity: Yes 
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Find proteins for P09471 (Homo sapiens)
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Go to UniProtKB:  P09471
PHAROS:  P09471
GTEx:  ENSG00000087258 
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UniProt GroupP09471
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1349Mus musculusMutation(s): 0 
Gene Names: Gnb1
UniProt & NIH Common Fund Data Resources
Find proteins for P62874 (Mus musculus)
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Go to UniProtKB:  P62874
IMPC:  MGI:95781
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UniProt GroupP62874
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2C [auth G]71Homo sapiensMutation(s): 0 
Gene Names: GNG2
Membrane Entity: Yes 
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Find proteins for P59768 (Homo sapiens)
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PHAROS:  P59768
GTEx:  ENSG00000186469 
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UniProt GroupP59768
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Alpha-2A adrenergic receptor,Endolysin,Alpha-2B adrenergic receptor,Alpha-2B adrenergic receptorD [auth R]512Bos taurusEnterobacteria phage RB59Homo sapiensMutation(s): 0 
Gene Names: ADRA2AeRB59_126ADRA2BADRA2L1ADRA2RL1
EC: 3.2.1.17
Membrane Entity: Yes 
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Find proteins for Q28838 (Bos taurus)
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Go to UniProtKB:  Q28838
Find proteins for P18089 (Homo sapiens)
Explore P18089 
Go to UniProtKB:  P18089
PHAROS:  P18089
GTEx:  ENSG00000274286 
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UniProt GroupsP18089Q28838
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
scFvE [auth H]307Mus musculusMutation(s): 0 
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
CZX
Query on CZX

Download Ideal Coordinates CCD File 
F [auth R]4-[(1~{S})-1-(2,3-dimethylphenyl)ethyl]-1~{H}-imidazole
C13 H16 N2
CUHVIMMYOGQXCV-NSHDSACASA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.90 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2020-04-15
    Type: Initial release
  • Version 1.1: 2020-05-06
    Changes: Database references
  • Version 1.2: 2020-05-13
    Changes: Structure summary