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1omw
From Proteopedia
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<StructureSection load='1omw' size='340' side='right'caption='[[1omw]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1omw' size='340' side='right'caption='[[1omw]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1omw]] is a 3 chain structure with sequence from [ | + | <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> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | + | <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> | |
| - | <tr id=' | + | <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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</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). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bos taurus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Capel | + | [[Category: Capel WD]] |
| - | [[Category: Lefkowitz | + | [[Category: Lefkowitz RJ]] |
| - | [[Category: Lodowski | + | [[Category: Lodowski DT]] |
| - | [[Category: Pitcher | + | [[Category: Pitcher JA]] |
| - | [[Category: Tesmer | + | [[Category: Tesmer JJG]] |
| - | + | ||
| - | + | ||
Current revision
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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