Beta-adrenergic receptor kinase

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<StructureSection load='' size='350' side='right' caption='Human BARK1 complex with RNA and Mg+2 ion (green) (PDB code [[3uzt]])' scene='70/705677/Cv/1'>
<StructureSection load='' size='350' side='right' caption='Human BARK1 complex with RNA and Mg+2 ion (green) (PDB code [[3uzt]])' scene='70/705677/Cv/1'>
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'''Beta adrenergic receptor kinase''' (BARK) is an intracellular serine/threonine kinase. BARK is activated by protein kinase A. BARK phosphorylates the β adregenic receptor (BAR) when it is occupied by the agonist thus causing its desensitization. BARK belongs to the family of G protein-coupled receptor kinase (GRK). <ref>PMID:2871555</ref>
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'''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. <ref>PMID:2871555</ref>
<scene name='70/705677/Cv/2'>Human BARK1 complex with RNA and Mg+2 ion</scene>;
<scene name='70/705677/Cv/2'>Human BARK1 complex with RNA and Mg+2 ion</scene>;

Revision as of 19:23, 15 January 2018

Human BARK1 complex with RNA and Mg+2 ion (green) (PDB code 3uzt)

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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

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