Beta-adrenergic receptor kinase

From Proteopedia

Revision as of 19:23, 15 January 2018

spinqualitylabelsall models Human BARK1 complex with RNA and Mg+2 ion (green) (PDB code 3uzt) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Beta adrenergic receptor kinase (BARK), currently termned GRK2 for G protein-coupled receptor kinase 2, is an intracellular serine/threonine kinase. BARK is activated by protein kinase A. BARK phosphorylates the β adregenic receptor (BAR), as well as many other G protein-coupled receptors, when it is occupied by the agonist thus causing its desensitization. BARK belongs to the family of G protein-coupled receptor kinases (GRK) that encompases 5 diferent isozymes. [1] ; (PDB code 3uzt).[2]

3D Structures of β adrenergic receptor kinase

Updated on 15-January-2018

1ym7 – bBARK1 (mutant) - bovine
4pnk, 3cik, 5he3 – hBARK1 + guanine-nucleotide binding protein G β,γ subunits – human
3psc, 5he0, 5he1, 5he2 – hBARK1 (mutant) + guanine-nucleotide binding protein G β,γ subunits
4mk0, 3v5w – hBARK1 + guanine-nucleotide binding protein G β,γ subunits + paroxetine derivative
3uzs – hBARK1 (mutant) + guanine-nucleotide binding protein G β,γ subunits + RNA
3uzt – hBARK1 (mutant) + RNA
3krw, 3krx – hBARK1 + guanine-nucleotide binding protein G β,γ subunits + inhibitor
3pvu, 3pvw – bBARK1 (mutant) + guanine-nucleotide binding protein G β,γ subunits + inhibitor
2bcj – bBARK1 (mutant) + guanine-nucleotide binding protein G α,β,γ subunits
1omw – bBARK1 (mutant) + guanine-nucleotide binding protein G β,γ subunits

References

1. ↑ Benovic JL, Strasser RH, Caron MG, Lefkowitz RJ. Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor. Proc Natl Acad Sci U S A. 1986 May;83(9):2797-801. PMID:2871555
2. ↑ Tesmer VM, Lennarz S, Mayer G, Tesmer JJ. Molecular Mechanism for Inhibition of G Protein-Coupled Receptor Kinase 2 by a Selective RNA Aptamer. Structure. 2012 Jun 21. PMID:22727813 doi:10.1016/j.str.2012.05.002