3c4w: Difference between revisions
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==Crystal Structure of G protein coupled receptor kinase 1 bound to ATP and magnesium chloride at 2.7A== | ==Crystal Structure of G protein coupled receptor kinase 1 bound to ATP and magnesium chloride at 2.7A== | ||
<StructureSection load='3c4w' size='340' side='right' caption='[[3c4w]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='3c4w' size='340' side='right' caption='[[3c4w]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRK1, RHOK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRK1, RHOK ([http://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'>[http://en.wikipedia.org/wiki/Rhodopsin_kinase Rhodopsin kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.14 2.7.11.14] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Rhodopsin_kinase Rhodopsin kinase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c4w OCA], [http://pdbe.org/3c4w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c4w RCSB], [http://www.ebi.ac.uk/pdbsum/3c4w PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c4w OCA], [http://pdbe.org/3c4w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c4w RCSB], [http://www.ebi.ac.uk/pdbsum/3c4w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c4w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c4/3c4w_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c4/3c4w_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 16:11, 7 November 2018
Crystal Structure of G protein coupled receptor kinase 1 bound to ATP and magnesium chloride at 2.7ACrystal Structure of G protein coupled receptor kinase 1 bound to ATP and magnesium chloride at 2.7A
Structural highlights
Function[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). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedG protein-coupled receptor (GPCR) kinases (GRKs) phosphorylate activated heptahelical receptors, leading to their uncoupling from G proteins. Here we report six crystal structures of rhodopsin kinase (GRK1), revealing not only three distinct nucleotide-binding states of a GRK but also two key structural elements believed to be involved in the recognition of activated GPCRs. The first is the C-terminal extension of the kinase domain, which was observed in all nucleotide-bound GRK1 structures. The second is residues 5-30 of the N terminus, observed in one of the GRK1.(Mg2+)2.ATP structures. The N terminus was also clearly phosphorylated, leading to the identification of two novel phosphorylation sites by mass spectral analysis. Co-localization of the N terminus and the C-terminal extension near the hinge of the kinase domain suggests that activated GPCRs stimulate kinase activity by binding to this region to facilitate full closure of the kinase domain. Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation.,Singh P, Wang B, Maeda T, Palczewski K, Tesmer JJ J Biol Chem. 2008 May 16;283(20):14053-62. Epub 2008 Mar 13. PMID:18339619[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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