Beta-adrenergic receptor kinase
From Proteopedia
(Difference between revisions)
(New page: <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> Beta adrenergic receptor kinase (BARK) is an intracellular serine/threonine kinase. B...) |
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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'> | ||
| + | '''Beta adrenergic receptor kinase''' or '''G-protein coupled 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 adrenergic receptor (BAR) as well as many other G protein-coupled receptors when they are 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/4'>Human BARK1 complex with RNA and Mg+2 ion</scene>; |
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| - | = | + | <scene name='70/705677/Cv/5'>Mg+2 ion coordination site</scene> (PDB code [[3uzt]]).<ref>PMID:22727813</ref> |
| - | == | + | == 3D Structures of β adrenergic receptor kinase == |
| + | [[Beta adrenergic receptor kinase 3D structures]] | ||
| - | + | </StructureSection> | |
| - | == Structural highlights == | ||
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| - | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
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| - | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
| + | [[Category:Topic Page]] | ||
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References
- ↑ 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
- ↑ 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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