2BCJ

Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-q and Gbetagamma Subunits


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.06 Å
  • R-Value Free: 0.292 
  • R-Value Work: 0.243 
  • R-Value Observed: 0.236 

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This is version 1.4 of the entry. See complete history


Literature

Snapshot of Activated G Proteins at the Membrane: The Gq-GRK2-G Complex

Tesmer, V.M.Kawano, T.Shankaranarayanan, A.Kozasa, T.Tesmer, J.J.G.

(2005) Science 310: 1686-1690

  • DOI: https://doi.org/10.1126/science.1118890
  • Primary Citation of Related Structures:  
    2BCJ

  • PubMed Abstract: 

    G protein-coupled receptor kinase 2 (GRK2) plays a key role in the desensitization of G protein-coupled receptor signaling by phosphorylating activated heptahelical receptors and by sequestering heterotrimeric G proteins. We report the atomic structure of GRK2 in complex with Galphaq and Gbetagamma, in which the activated Galpha subunit of Gq is fully dissociated from Gbetagamma and dramatically reoriented from its position in the inactive Galphabetagamma heterotrimer. Galphaq forms an effector-like interaction with the GRK2 regulator of G protein signaling (RGS) homology domain that is distinct from and does not overlap with that used to bind RGS proteins such as RGS4.


  • Organizational Affiliation

    Institute for Cellular and Molecular Biology, Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, TX 78712, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
G-protein-coupled receptor kinase 2689Bos taurusMutation(s): 1 
Gene Names: GRK2ADRBK1
EC: 2.7.11.15
Membrane Entity: Yes 
UniProt
Find proteins for P21146 (Bos taurus)
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Go to UniProtKB:  P21146
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UniProt GroupP21146
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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-1340Bos taurusMutation(s): 1 
Gene Names: GNB1
UniProt
Find proteins for P62871 (Bos taurus)
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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]71Bos taurusMutation(s): 1 
Gene Names: GNG2
Membrane Entity: Yes 
UniProt
Find proteins for P63212 (Bos taurus)
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Guanine nucleotide-binding protein G(i) subunit alpha-1, Guanine nucleotide-binding protein G(q) subunit alpha chimeraD [auth Q]353Rattus norvegicusMus musculus
This entity is chimeric
Mutation(s): 0 
Gene Names: Gnai1Gnai-1Gnaq
Membrane Entity: Yes 
UniProt
Find proteins for P10824 (Rattus norvegicus)
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Find proteins for P21279 (Mus musculus)
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UniProt GroupsP21279P10824
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Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.06 Å
  • R-Value Free: 0.292 
  • R-Value Work: 0.243 
  • R-Value Observed: 0.236 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 64.918α = 90
b = 129.954β = 95.81
c = 122.764γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
PDB_EXTRACTdata extraction
HKL-2000data reduction
SCALEPACKdata scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-12-20
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.3: 2017-06-28
    Changes: Database references, Source and taxonomy, Structure summary
  • Version 1.4: 2023-08-23
    Changes: Data collection, Database references, Derived calculations, Refinement description