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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:
    Journal Article
  • Authors:
    Lodowski DT, Barnhill JF, Pitcher JA, Capel WD, Lefkowitz RJ, Tesmer JJ
  • Publication date:
    05/2003
  • Pagination:
    936, 939
  • Journal:
    Acta Crystallogr D Biol Crystallogr
  • Volume:
    59
  • Issue:
    Pt 5
  • Country:
    Denmark
  • Print ISSN:
    0907-4449
  • PII:
    S0907444903002622
  • Language:
    eng
  • Keywords:
    Animals, Cattle, Cell Line, Crystallization, Cyclic AMP-Dependent Protein Kinases, Heterotrimeric GTP-Binding Proteins, Protein Subunits, Recombinant Proteins, Spodoptera, X-Ray Diffraction, beta-Adrenergic Receptor Kinases
Abstract
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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