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| | <StructureSection load='3t8o' size='340' side='right'caption='[[3t8o]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='3t8o' size='340' side='right'caption='[[3t8o]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3t8o]] is a 1 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=3T8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T8O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3t8o]] is a 1 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=3T8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T8O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3c4w|3c4w]], [[3c4x|3c4x]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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='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=3t8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t8o OCA], [https://pdbe.org/3t8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t8o RCSB], [https://www.ebi.ac.uk/pdbsum/3t8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t8o 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=3t8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t8o OCA], [https://pdbe.org/3t8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t8o RCSB], [https://www.ebi.ac.uk/pdbsum/3t8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t8o 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 kinase 1 (GRK1 or rhodopsin kinase) phosphorylates activated rhodopsin and initiates a cascade of events that results in the termination of phototransduction by the receptor. Although GRK1 seems to be a monomer in solution, seven prior crystal structures of GRK1 revealed a similar domain-swapped dimer interface involving the C-terminus of the enzyme. The influence of this interface on the overall conformation of GRK1 is not known. To address this question, the crystalline dimer interface was disrupted with a L166K mutation and the structure of GRK1-L166K was determined in complex with Mg(2+) . ATP to 2.5 A resolution. GRK1-L166K crystallized in a novel space group as a monomer and exhibited little overall conformational difference from prior structures of GRK1, although the C-terminal domain-swapped region had reorganized owing to loss of the dimer interface.
| + | |
| - | | + | |
| - | Structure of a monomeric variant of rhodopsin kinase at 2.5 A resolution.,Tesmer JJ, Nance MR, Singh P, Lee H Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):622-5. doi:, 10.1107/S1744309112017435. Epub 2012 May 22. PMID:22684056<ref>PMID:22684056</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div> | + | |
| - | <div class="pdbe-citations 3t8o" 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: Nance MR]] |
| - | [[Category: Nance, M R]] | + | [[Category: Singh P]] |
| - | [[Category: Singh, P]] | + | [[Category: Tesmer JJG]] |
| - | [[Category: Tesmer, J J.G]] | + | |
| - | [[Category: Kinase domain]]
| + | |
| - | [[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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