Beta-adrenergic receptor kinase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 2: Line 2:
'''Beta adrenergic receptor kinase''' (BARK), currently termed 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 they is occupied by the agonist thus causing their desensitization. BARK belongs to the family of G protein-coupled receptor kinases (GRK) that encompases 5 different isozymes. <ref>PMID:2871555</ref>
'''Beta adrenergic receptor kinase''' (BARK), currently termed 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 they is occupied by the agonist thus causing their desensitization. BARK belongs to the family of G protein-coupled receptor kinases (GRK) that encompases 5 different 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/4'>Human BARK1 complex with RNA and Mg+2 ion</scene>;
-
<scene name='70/705677/Cv/3'>Mg+2 ion coordination site</scene> (PDB code [[3uzt]]).<ref>PMID:22727813</ref>
+
<scene name='70/705677/Cv/5'>Mg+2 ion coordination site</scene> (PDB code [[3uzt]]).<ref>PMID:22727813</ref>
</StructureSection>
</StructureSection>
== 3D Structures of β adrenergic receptor kinase ==
== 3D Structures of β adrenergic receptor kinase ==

Revision as of 10:50, 17 May 2018

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

Drag the structure with the mouse to rotate

3D Structures of β adrenergic receptor kinase

Updated on 17-May-2018

1ym7 – bBARK1 (mutant) - bovine
5uvc, 5uuu – hBARK1 + inhibitor - human
4pnk, 3cik, 5he3 – hBARK1 + guanine-nucleotide binding protein G β,γ subunits
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, 5wg3, 5wg4, 5wg5, 5ukk, 5ukl, 5he3 – hBARK1 + guanine-nucleotide binding protein G β,γ subunits + inhibitor
3pvu, 3pvw, 5ukm, 5he0, 5he1, 5he2 – 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Cristina Murga, Joel L. Sussman

Personal tools