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==Structure of the C13.18 RNA Aptamer in Complex with G Protein-Coupled Receptor Kinase 2== | ==Structure of the C13.18 RNA Aptamer in Complex with G Protein-Coupled Receptor Kinase 2== | ||
<StructureSection load='3uzt' size='340' side='right' caption='[[3uzt]], [[Resolution|resolution]] 3.51Å' scene=''> | <StructureSection load='3uzt' size='340' side='right'caption='[[3uzt]], [[Resolution|resolution]] 3.51Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3uzt]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3uzt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UZT FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3uzs|3uzs]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3uzs|3uzs]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADRBK1, GRK2 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADRBK1, GRK2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/[Beta-adrenergic-receptor]_kinase [Beta-adrenergic-receptor] kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.15 2.7.11.15] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3uzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uzt OCA], [https://pdbe.org/3uzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uzt RCSB], [https://www.ebi.ac.uk/pdbsum/3uzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uzt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/ARBK1_BOVIN ARBK1_BOVIN]] Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them. Key regulator of LPAR1 signaling. Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor. Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 23: | Line 23: | ||
==See Also== | ==See Also== | ||
*[[Beta adrenergic receptor kinase 3D structures|Beta adrenergic receptor kinase 3D structures]] | |||
*[[Beta-adrenergic receptor kinase|Beta-adrenergic receptor kinase]] | *[[Beta-adrenergic receptor kinase|Beta-adrenergic receptor kinase]] | ||
== References == | == References == | ||
| Line 29: | Line 30: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bovin]] | [[Category: Bovin]] | ||
[[Category: Large Structures]] | |||
[[Category: Tesmer, J J.G]] | [[Category: Tesmer, J J.G]] | ||
[[Category: Tesmer, V M]] | [[Category: Tesmer, V M]] | ||
Revision as of 11:18, 20 July 2022
Structure of the C13.18 RNA Aptamer in Complex with G Protein-Coupled Receptor Kinase 2Structure of the C13.18 RNA Aptamer in Complex with G Protein-Coupled Receptor Kinase 2
Structural highlights
Function[ARBK1_BOVIN] Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them. Key regulator of LPAR1 signaling. Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor. Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner (By similarity). Publication Abstract from PubMedCardiovascular homeostasis is maintained in part by the rapid desensitization of activated heptahelical receptors that have been phosphorylated by G protein-coupled receptor kinase 2 (GRK2). However, during chronic heart failure GRK2 is upregulated and believed to contribute to disease progression. We have determined crystallographic structures of GRK2 bound to an RNA aptamer that potently and selectively inhibits kinase activity. Key to the mechanism of inhibition is the positioning of an adenine nucleotide into the ATP-binding pocket and interactions with the basic alphaF-alphaG loop region of the GRK2 kinase domain. Constraints imposed on the RNA by the terminal stem of the aptamer also play a role. These results highlight how a high-affinity aptamer can be used to selectively trap a novel conformational state of a protein kinase. Molecular Mechanism for Inhibition of G Protein-Coupled Receptor Kinase 2 by a Selective RNA Aptamer.,Tesmer VM, Lennarz S, Mayer G, Tesmer JJ Structure. 2012 Jun 21. PMID:22727813[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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