Purification, crystallization and preliminary X-ray diffraction studies of a complex between G protein-coupled receptor kinase 2 and Gbeta1gamma2.
| dc.contributor.author | Lodowski, David T | |
| dc.contributor.author | Barnhill, Jennifer F | |
| dc.contributor.author | Pitcher, Julie A | |
| dc.contributor.author | Capel, W Darrell | |
| dc.contributor.author | Lefkowitz, Robert J | |
| dc.contributor.author | Tesmer, John JG | |
| dc.coverage.spatial | United States | |
| dc.date.accessioned | 2013-09-05T15:33:08Z | |
| dc.date.issued | 2003-05 | |
| dc.description.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. | |
| dc.identifier | ||
| dc.identifier | S0907444903002622 | |
| dc.identifier.issn | 0907-4449 | |
| dc.identifier.uri | ||
| dc.language | eng | |
| dc.publisher | International Union of Crystallography (IUCr) | |
| dc.relation.ispartof | Acta Crystallogr D Biol Crystallogr | |
| dc.subject | Animals | |
| dc.subject | Cattle | |
| dc.subject | Cell Line | |
| dc.subject | Crystallization | |
| dc.subject | Cyclic AMP-Dependent Protein Kinases | |
| dc.subject | Heterotrimeric GTP-Binding Proteins | |
| dc.subject | Protein Subunits | |
| dc.subject | Recombinant Proteins | |
| dc.subject | Spodoptera | |
| dc.subject | X-Ray Diffraction | |
| dc.subject | beta-Adrenergic Receptor Kinases | |
| dc.title | Purification, crystallization and preliminary X-ray diffraction studies of a complex between G protein-coupled receptor kinase 2 and Gbeta1gamma2. | |
| dc.type | Journal article | |
| pubs.author-url | ||
| pubs.begin-page | 936 | |
| pubs.end-page | 939 | |
| pubs.issue | Pt 5 | |
| pubs.organisational-group | Basic Science Departments | |
| pubs.organisational-group | Biochemistry | |
| pubs.organisational-group | Chemistry | |
| pubs.organisational-group | Clinical Science Departments | |
| pubs.organisational-group | Duke | |
| pubs.organisational-group | Duke Cancer Institute | |
| pubs.organisational-group | Institutes and Centers | |
| pubs.organisational-group | Medicine | |
| pubs.organisational-group | Medicine, Cardiology | |
| pubs.organisational-group | Pathology | |
| pubs.organisational-group | School of Medicine | |
| pubs.organisational-group | Trinity College of Arts & Sciences | |
| pubs.publication-status | Published | |
| pubs.volume | 59 |
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