1omw

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[[Image:1omw.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of the complex between G Protein-Coupled Receptor Kinase 2 and Heterotrimeric G Protein beta 1 and gamma 2 subunits==
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|PDB= 1omw |SIZE=350|CAPTION= <scene name='initialview01'>1omw</scene>, resolution 2.50&Aring;
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<StructureSection load='1omw' size='340' side='right'caption='[[1omw]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CMT:O-METHYLCYSTEINE'>CMT</scene>
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<table><tr><td colspan='2'>[[1omw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OMW FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/[Beta-adrenergic-receptor]_kinase [Beta-adrenergic-receptor] kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.15 2.7.11.15] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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|GENE= GRK2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]), GNB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]), GNG2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMT:O-METHYLCYSTEINE'>CMT</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1omw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omw OCA], [https://pdbe.org/1omw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1omw RCSB], [https://www.ebi.ac.uk/pdbsum/1omw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1omw ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1omw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omw OCA], [http://www.ebi.ac.uk/pdbsum/1omw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1omw RCSB]</span>
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== Function ==
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}}
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/om/1omw_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1omw ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The phosphorylation of heptahelical receptors by heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptor kinases (GRKs) is a universal regulatory mechanism that leads to desensitization of G protein signaling and to the activation of alternative signaling pathways.We determined the crystallographic structure of bovine GRK2 in complex with G protein beta1gamma2 subunits.Our results show how the three domains of GRK2-the RGS (regulator of G protein signaling) homology, protein kinase, and pleckstrin homology domains-integrate their respective activities and recruit the enzyme to the cell membrane in an orientation that not only facilitates receptor phosphorylation, but also allows for the simultaneous inhibition of signaling by Galpha and Gbetagamma subunits.
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'''Crystal Structure of the complex between G Protein-Coupled Receptor Kinase 2 and Heterotrimeric G Protein beta 1 and gamma 2 subunits'''
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Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and Gbetagamma.,Lodowski DT, Pitcher JA, Capel WD, Lefkowitz RJ, Tesmer JJ Science. 2003 May 23;300(5623):1256-62. PMID:12764189<ref>PMID:12764189</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1omw" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The phosphorylation of heptahelical receptors by heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptor kinases (GRKs) is a universal regulatory mechanism that leads to desensitization of G protein signaling and to the activation of alternative signaling pathways.We determined the crystallographic structure of bovine GRK2 in complex with G protein beta1gamma2 subunits.Our results show how the three domains of GRK2-the RGS (regulator of G protein signaling) homology, protein kinase, and pleckstrin homology domains-integrate their respective activities and recruit the enzyme to the cell membrane in an orientation that not only facilitates receptor phosphorylation, but also allows for the simultaneous inhibition of signaling by Galpha and Gbetagamma subunits.
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*[[Beta adrenergic receptor kinase 3D structures|Beta adrenergic receptor kinase 3D structures]]
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*[[Transducin 3D structures|Transducin 3D structures]]
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==About this Structure==
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== References ==
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1OMW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMW OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and Gbetagamma., Lodowski DT, Pitcher JA, Capel WD, Lefkowitz RJ, Tesmer JJ, Science. 2003 May 23;300(5623):1256-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12764189 12764189]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: [Beta-adrenergic-receptor] kinase]]
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[[Category: Capel WD]]
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[[Category: Capel, W D.]]
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[[Category: Lefkowitz RJ]]
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[[Category: Lefkowitz, R J.]]
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[[Category: Lodowski DT]]
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[[Category: Lodowski, D T.]]
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[[Category: Pitcher JA]]
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[[Category: Pitcher, J A.]]
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[[Category: Tesmer JJG]]
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[[Category: Tesmer, J J.G.]]
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[[Category: wd-40 repeat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:47:32 2008''
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Current revision

Crystal Structure of the complex between G Protein-Coupled Receptor Kinase 2 and Heterotrimeric G Protein beta 1 and gamma 2 subunits

PDB ID 1omw

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