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Purification, crystallization and preliminary X-ray diffraction studies of a complex between G protein-coupled receptor kinase 2 and Gbeta1gamma2.

Publication ,  Journal Article
Lodowski, DT; Barnhill, JF; Pitcher, JA; Capel, WD; Lefkowitz, RJ; Tesmer, JJG
Published in: Acta Crystallogr D Biol Crystallogr
May 2003

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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Published In

Acta Crystallogr D Biol Crystallogr

DOI

ISSN

0907-4449

Publication Date

May 2003

Volume

59

Issue

Pt 5

Start / End Page

936 / 939

Location

United States

Related Subject Headings

  • beta-Adrenergic Receptor Kinases
  • X-Ray Diffraction
  • Spodoptera
  • Recombinant Proteins
  • Protein Subunits
  • Heterotrimeric GTP-Binding Proteins
  • Cyclic AMP-Dependent Protein Kinases
  • Crystallization
  • Cell Line
  • Cattle
 

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Lodowski, D. T., Barnhill, J. F., Pitcher, J. A., Capel, W. D., Lefkowitz, R. J., & Tesmer, J. J. G. (2003). Purification, crystallization and preliminary X-ray diffraction studies of a complex between G protein-coupled receptor kinase 2 and Gbeta1gamma2. Acta Crystallogr D Biol Crystallogr, 59(Pt 5), 936–939. https://doi.org/10.1107/s0907444903002622
Lodowski, David T., Jennifer F. Barnhill, Julie A. Pitcher, W Darrell Capel, Robert J. Lefkowitz, and John J. G. Tesmer. “Purification, crystallization and preliminary X-ray diffraction studies of a complex between G protein-coupled receptor kinase 2 and Gbeta1gamma2.Acta Crystallogr D Biol Crystallogr 59, no. Pt 5 (May 2003): 936–39. https://doi.org/10.1107/s0907444903002622.
Lodowski DT, Barnhill JF, Pitcher JA, Capel WD, Lefkowitz RJ, Tesmer JJG. Purification, crystallization and preliminary X-ray diffraction studies of a complex between G protein-coupled receptor kinase 2 and Gbeta1gamma2. Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):936–9.
Lodowski, David T., et al. “Purification, crystallization and preliminary X-ray diffraction studies of a complex between G protein-coupled receptor kinase 2 and Gbeta1gamma2.Acta Crystallogr D Biol Crystallogr, vol. 59, no. Pt 5, May 2003, pp. 936–39. Pubmed, doi:10.1107/s0907444903002622.
Lodowski DT, Barnhill JF, Pitcher JA, Capel WD, Lefkowitz RJ, Tesmer JJG. Purification, crystallization and preliminary X-ray diffraction studies of a complex between G protein-coupled receptor kinase 2 and Gbeta1gamma2. Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):936–939.
Journal cover image

Published In

Acta Crystallogr D Biol Crystallogr

DOI

ISSN

0907-4449

Publication Date

May 2003

Volume

59

Issue

Pt 5

Start / End Page

936 / 939

Location

United States

Related Subject Headings

  • beta-Adrenergic Receptor Kinases
  • X-Ray Diffraction
  • Spodoptera
  • Recombinant Proteins
  • Protein Subunits
  • Heterotrimeric GTP-Binding Proteins
  • Cyclic AMP-Dependent Protein Kinases
  • Crystallization
  • Cell Line
  • Cattle