1omw: Difference between revisions

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[[Image:1omw.png|left|200px]]


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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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<StructureSection load='1omw' size='340' side='right'caption='[[1omw]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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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<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>
{{STRUCTURE_1omw|  PDB=1omw  |  SCENE=  }}
<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>
</table>
== 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).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/om/1omw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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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== Publication Abstract from PubMed ==
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.


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


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1omw" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_12764189}}, adds the Publication Abstract to the page
*[[Beta adrenergic receptor kinase 3D structures|Beta adrenergic receptor kinase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 12764189 is the PubMed ID number.
*[[Transducin 3D structures|Transducin 3D structures]]
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== References ==
{{ABSTRACT_PUBMED_12764189}}
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
[[1omw]] is a 3 chain structure with sequence 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].
 
==Reference==
<ref group="xtra">PMID:012764189</ref><references group="xtra"/>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Capel, W D.]]
[[Category: Large Structures]]
[[Category: Lefkowitz, R J.]]
[[Category: Capel WD]]
[[Category: Lodowski, D T.]]
[[Category: Lefkowitz RJ]]
[[Category: Pitcher, J A.]]
[[Category: Lodowski DT]]
[[Category: Tesmer, J J.G.]]
[[Category: Pitcher JA]]
[[Category: Transferase]]
[[Category: Tesmer JJG]]
[[Category: Wd-40 repeat]]

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