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

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Lodowski, DT; Barnhill, JF; Pitcher, JA; Capel, WD; Lefkowitz, RJ; Tesmer, JJG

Published Date

  • May 2003

Published In

Volume / Issue

  • 59 / Pt 5

Start / End Page

  • 936 - 939

PubMed ID

  • 12777817

Pubmed Central ID

  • 12777817

Electronic International Standard Serial Number (EISSN)

  • 1399-0047

International Standard Serial Number (ISSN)

  • 0907-4449

Digital Object Identifier (DOI)

  • 10.1107/s0907444903002622

Language

  • eng