Purification, crystallization and preliminary X-ray diffraction studies of a complex between G protein-coupled receptor kinase 2 and Gβ1γ2
| Autor: | Jennifer F. Barnhill, Julie A. Pitcher, David T. Lodowski, W. Darrell Capel, Robert J. Lefkowitz, John J.G. Tesmer |
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| Rok vydání: | 2003 |
| Předmět: |
Stereochemistry
Protein subunit Spodoptera Cell Line chemistry.chemical_compound X-Ray Diffraction Structural Biology Heterotrimeric G protein Animals Receptor G protein-coupled receptor G protein-coupled receptor kinase biology Beta adrenergic receptor kinase CHAPS detergent General Medicine Cyclic AMP-Dependent Protein Kinases Heterotrimeric GTP-Binding Proteins Recombinant Proteins Protein Subunits G beta-gamma complex Crystallography chemistry beta-Adrenergic Receptor Kinases biology.protein Cattle Crystallization |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 59:936-939 |
| ISSN: | 0907-4449 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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