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Publication Detail
Purification, crystallization and preliminary X-ray diffraction studies of a complex between G protein-coupled receptor kinase 2 and Gbeta1gamma2.
  • Publication Type:
    Journal article
  • Publication Sub Type:
  • Authors:
    Lodowski DT, Barnhill JF, Pitcher JA, Capel WD, Lefkowitz RJ, Tesmer JJ
  • Publisher:
    International Union of Crystallography
  • Publication date:
  • Pagination:
    936, 939
  • Journal:
    Acta Crystallographica Section D
  • Volume:
  • Issue:
  • Print ISSN:
  • Addresses:
    Institute for Cellular and Molecular Biology, Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, TX, USA.
G protein-coupled receptor kinase 2 (GRK2) phosphorylates activated G protein-coupled receptors (GPCRs), which ultimately leads to their desensitization and/or downregulation. The enzyme is recruited to the plasma membrane via the interaction of its carboxyl-terminal pleckstrin-homology (PH) domain with the beta and gamma subunits of heterotrimeric G proteins (Gbetagamma). An improved purification scheme for GRK2 has been developed, conditions under which GRK2 forms a complex with Gbeta(1)gamma(2) have been determined and the complex has been crystallized in CHAPS detergent micelles. Crystals of the GRK2-Gbetagamma complex belong to space group C2 and have unit-cell parameters a = 187.0, b = 72.1, c = 122.0 A, beta = 115.2 degrees. A complete data set has been collected to 3.2 A resolution with Cu Kalpha radiation.
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