3C4X

Crystal Structure of G protein coupled receptor kinase 1 bound to ATP and magnesium chloride at 2.9A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Work: 0.193 
  • R-Value Observed: 0.193 

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This is version 1.2 of the entry. See complete history


Literature

Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation.

Singh, P.Wang, B.Maeda, T.Palczewski, K.Tesmer, J.J.

(2008) J Biol Chem 283: 14053-14062

  • DOI: https://doi.org/10.1074/jbc.M708974200
  • Primary Citation of Related Structures:  
    3C4W, 3C4X, 3C4Y, 3C4Z, 3C50, 3C51

  • PubMed Abstract: 

    G protein-coupled receptor (GPCR) kinases (GRKs) phosphorylate activated heptahelical receptors, leading to their uncoupling from G proteins. Here we report six crystal structures of rhodopsin kinase (GRK1), revealing not only three distinct nucleotide-binding states of a GRK but also two key structural elements believed to be involved in the recognition of activated GPCRs. The first is the C-terminal extension of the kinase domain, which was observed in all nucleotide-bound GRK1 structures. The second is residues 5-30 of the N terminus, observed in one of the GRK1.(Mg2+)2.ATP structures. The N terminus was also clearly phosphorylated, leading to the identification of two novel phosphorylation sites by mass spectral analysis. Co-localization of the N terminus and the C-terminal extension near the hinge of the kinase domain suggests that activated GPCRs stimulate kinase activity by binding to this region to facilitate full closure of the kinase domain.


  • Organizational Affiliation

    Life Sciences Institute, Department of Pharmacology, University of Michigan, Ann Arbor, Michigan 48109-2216, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Rhodopsin kinase
A, B
543Bos taurusMutation(s): 0 
Gene Names: GRK1RHOK
EC: 2.7.11.14
UniProt
Find proteins for P28327 (Bos taurus)
Explore P28327 
Go to UniProtKB:  P28327
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP28327
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Work: 0.193 
  • R-Value Observed: 0.193 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 54.116α = 90
b = 95.122β = 90
c = 234.823γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-03-11
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Refinement description