Literature summary for 2.7.11.15 extracted from

Lodowski, D.T.; Barnhill, J.F.; Pitcher, J.A.; Capel, W.D.; Lefkowitz, R.J.; Tesmer, J.J.
Purification, crystallization and preliminary X-ray diffraction studies of a complex between G protein-coupled receptor kinase 2 and Gbeta1gamma2 (2003), Acta Crystallogr. Sect. D, 59, 936-939.

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Activating Compound

Activating Compound	Comment	Organism	Structure
G protein	GRK2 binds G protein beta1gamma2 subunits, binding structure, no correct complex formation with recombinant Gbetagamma mutant C68S lacking the isoprenylation site, overview	Bos taurus

Cloned(Commentary)

Cloned (Comment)	Organism
co-overexpression of GRK2 and His6-tagged G protein beta1gamma2 subunits in Spodoptera frugiperda Sf9 cells using the baculovirus infection system	Bos taurus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant GRK2 in complex with purified recombinant bovine G protein beta1gamma2 subunits, two-dimensional hanging drop vapor diffusion method screen, 0.001 ml protein solution containing 5-20% PEG3350 versus pH 5.0-7.5, 1 M NaCl, 12 mg/ml protein, mixed with 0.001 ml of well solution containing 0.1 M MES, pH 5.25, 0.2 M NaCl, 1 mM inositol-3,4,5-trisphosphate, 5 mM MgCl2, and 6.9-7.8% PEG3350, versus 1 ml of well solution, inositol-3,4,5-trisphosphate can be substituted by EDTA and phosphatidylserine, both crystal types diffract differently but show identical unit-cell parameters, X-ray diffraction structure determination and analysis at 3.2 A resolution, Cu Kalpha radiation	Bos taurus

Crystallization (Comment)

Organism

purified recombinant GRK2 in complex with purified recombinant bovine G protein beta1gamma2 subunits, two-dimensional hanging drop vapor diffusion method screen, 0.001 ml protein solution containing 5-20% PEG3350 versus pH 5.0-7.5, 1 M NaCl, 12 mg/ml protein, mixed with 0.001 ml of well solution containing 0.1 M MES, pH 5.25, 0.2 M NaCl, 1 mM inositol-3,4,5-trisphosphate, 5 mM MgCl2, and 6.9-7.8% PEG3350, versus 1 ml of well solution, inositol-3,4,5-trisphosphate can be substituted by EDTA and phosphatidylserine, both crystal types diffract differently but show identical unit-cell parameters, X-ray diffraction structure determination and analysis at 3.2 A resolution, Cu Kalpha radiation

Bos taurus

Inhibitors

Inhibitors	Comment	Organism	Structure
EDTA	-	Bos taurus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	associated, GRK2 in complex with G protein beta1gamma2 subunits	Bos taurus	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Bos taurus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
80000	-	x * 80000, recombinant GRK2, gel filtration and SDS-PAGE	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant GRK2 from Spodoptera frugiperda Sf9 cells to near homogeneity by ultracentrifugation, 3 steps of cation exchange chromatography, heparin affinity chromatography, another ion exchange chromatography step, and gel filtration, the recombinant His6-tagged G protein beta1gamma2 subunits by solubilization from membranes, Ni2+ affinity and ion exchange chromatography, and gel filtration	Bos taurus

Renatured (Commentary)

Renatured (Comment)	Organism
reconstitution of the GRK2-G protein beta1gamma2 subunits complex by mixing in a 2:3 ratio	Bos taurus

Subunits

Subunits	Comment	Organism
?	x * 80000, recombinant GRK2, gel filtration and SDS-PAGE	Bos taurus
More	GRK2 consists of 3 modular domains: a predominantly N-terminal RGS homology domain, a central protein kinase domain, and a C-terminal pleckstrin homology domain, domain functions, overview	Bos taurus

Synonyms

Synonyms	Comment	Organism
G protein-coupled receptor kinase 2	-	Bos taurus
GRK2	-	Bos taurus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Bos taurus