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| | <StructureSection load='3qc9' size='340' side='right'caption='[[3qc9]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='3qc9' size='340' side='right'caption='[[3qc9]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qc9]] is a 4 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=3QC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QC9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3qc9]] is a 4 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=3QC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QC9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRK1, RHOK ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Rhodopsin_kinase Rhodopsin kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.14 2.7.11.14] </span></td></tr> | + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qc9 OCA], [https://pdbe.org/3qc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qc9 RCSB], [https://www.ebi.ac.uk/pdbsum/3qc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qc9 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qc9 OCA], [https://pdbe.org/3qc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qc9 RCSB], [https://www.ebi.ac.uk/pdbsum/3qc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qc9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RK_BOVIN RK_BOVIN]] Retina-specific kinase involved in the signal turnoff via phosphorylation of rhodopsin (RHO), the G protein- coupled receptor that initiates the phototransduction cascade. This rapid desensitization is essential for scotopic vision and permits rapid adaptation to changes in illumination (By similarity).
| + | [https://www.uniprot.org/uniprot/GRK1_BOVIN GRK1_BOVIN] Retina-specific kinase involved in the signal turnoff via phosphorylation of rhodopsin (RHO), the G protein- coupled receptor that initiates the phototransduction cascade (PubMed:12686556, PubMed:16675451, PubMed:21299498). This rapid desensitization is essential for scotopic vision and permits rapid adaptation to changes in illumination (By similarity). May play a role in the maintenance of the outer nuclear layer in the retina (By similarity).[UniProtKB:Q9WVL4]<ref>PMID:12686556</ref> <ref>PMID:16675451</ref> <ref>PMID:21299498</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | G protein-coupled receptor kinases (GRKs) phosphorylate activated G protein-coupled receptors (GPCRs) to initiate receptor desensitization. In addition to the canonical phosphoacceptor site of the kinase domain, activated receptors bind to a distinct docking site that confers higher affinity and activates GRKs allosterically. Recent mutagenesis and structural studies support a model wherein receptor docking activates a GRK by stabilizing the interaction of its ~20 amino acid N-terminal region with the kinase domain. This interaction in turn stabilizes a closed, more active conformation of the enzyme. To investigate the importance of this interaction for the process of GRK activation, we first validated the functionality of the N-terminal region in rhodopsin kinase (GRK1) by site-directed mutagenesis and then introduced a disulfide bond to cross-link the N-terminal region of GRK1 with its specific binding site on the kinase domain. Characterization of the kinetic and biophysical properties of the cross-linked protein showed that disulfide bond formation greatly enhances the catalytic efficiency of the peptide phosphorylation, but receptor-dependent phosphorylation, Meta II stabilization, and inhibition of transducin activation were unaffected. These data indicate that the interaction of the N-terminal region with the kinase domain is important for GRK activation, but that it does not dictate the affinity of GRKs for activated receptors.
| + | |
| - | | + | |
| - | Activation of G protein-coupled receptor kinase 1 involves interactions between its N-terminal region and its kinase domain.,Huang CC, Orban T, Jastrzebska B, Palczewski K, Tesmer JJ Biochemistry. 2011 Jan 25. PMID:21265573<ref>PMID:21265573</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div> | + | |
| - | <div class="pdbe-citations 3qc9" style="background-color:#fffaf0;"></div> | + | |
| | | | |
| | ==See Also== | | ==See Also== |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Rhodopsin kinase]]
| + | [[Category: Huang C-C]] |
| - | [[Category: Huang, C C]] | + | [[Category: Tesmer JJG]] |
| - | [[Category: Tesmer, J J.G]] | + | |
| - | [[Category: Enkaryotic protein kinase fold]]
| + | |
| - | [[Category: Protein serine/threonine kinase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
GRK1_BOVIN Retina-specific kinase involved in the signal turnoff via phosphorylation of rhodopsin (RHO), the G protein- coupled receptor that initiates the phototransduction cascade (PubMed:12686556, PubMed:16675451, PubMed:21299498). This rapid desensitization is essential for scotopic vision and permits rapid adaptation to changes in illumination (By similarity). May play a role in the maintenance of the outer nuclear layer in the retina (By similarity).[UniProtKB:Q9WVL4][1] [2] [3]
See Also
References
- ↑ Weiergraber OH, Senin II, Philippov PP, Granzin J, Koch KW. Impact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin. J Biol Chem. 2003 Jun 20;278(25):22972-9. Epub 2003 Apr 9. PMID:12686556 doi:10.1074/jbc.M300447200
- ↑ Higgins MK, Oprian DD, Schertler GF. Recoverin binds exclusively to an amphipathic peptide at the N terminus of rhodopsin kinase, inhibiting rhodopsin phosphorylation without affecting catalytic activity of the kinase. J Biol Chem. 2006 Jul 14;281(28):19426-32. doi: 10.1074/jbc.M602203200. Epub 2006 , May 4. PMID:16675451 doi:http://dx.doi.org/10.1074/jbc.M602203200
- ↑ Zernii EY, Komolov KE, Permyakov SE, Kolpakova T, Dell'orco D, Poetzsch A, Knyazeva EL, Grigoriev II, Permyakov EA, Senin II, Philippov PP, Koch KW. Involvement of the recoverin C-terminal segment in recognition of the target enzyme rhodopsin kinase. Biochem J. 2011 Apr 15;435(2):441-50. doi: 10.1042/BJ20110013. PMID:21299498 doi:http://dx.doi.org/10.1042/BJ20110013
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