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| - | [[Image:1vqx.gif|left|200px]] | |
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| - | <!-- | + | ==ARRESTIN-BOUND NMR STRUCTURES OF THE PHOSPHORYLATED CARBOXY-TERMINAL DOMAIN OF RHODOPSIN, REFINED== |
| - | The line below this paragraph, containing "STRUCTURE_1vqx", creates the "Structure Box" on the page.
| + | <StructureSection load='1vqx' size='340' side='right'caption='[[1vqx]]' 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'>[[1vqx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tqk 1tqk]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VQX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VQX 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">Solution NMR</td></tr> |
| - | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> |
| - | {{STRUCTURE_1vqx| PDB=1vqx | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vqx OCA], [https://pdbe.org/1vqx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vqx RCSB], [https://www.ebi.ac.uk/pdbsum/1vqx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vqx ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/OPSD_BOVIN OPSD_BOVIN] Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal (By similarity).<ref>PMID:16908857</ref> <ref>PMID:17060607</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Phosphorylation of activated G-protein-coupled receptors and the subsequent binding of arrestin mark major molecular events of homologous desensitization. In the visual system, interactions between arrestin and the phosphorylated rhodopsin are pivotal for proper termination of visual signals. By using high resolution proton nuclear magnetic resonance spectroscopy of the phosphorylated C terminus of rhodopsin, represented by a synthetic 7-phosphopolypeptide, we show that the arrestin-bound conformation is a well ordered helix-loop structure connected to rhodopsin via a flexible linker. In a model of the rhodopsin-arrestin complex, the phosphates point in the direction of arrestin and form a continuous negatively charged surface, which is stabilized by a number of positively charged lysine and arginine residues of arrestin. Opposite to the mostly extended structure of the unphosphorylated C-terminal domain of rhodopsin, the arrestin-bound C-terminal helix is a compact domain that occupies a central position between the cytoplasmic loops and occludes the key binding sites of transducin. In conjunction with other binding sites, the helix-loop structure provides a mechanism of shielding phosphates in the center of the rhodopsin-arrestin complex and appears critical in guiding arrestin for high affinity binding with rhodopsin. |
| | | | |
| - | '''ARRESTIN-BOUND NMR STRUCTURES OF THE PHOSPHORYLATED CARBOXY-TERMINAL DOMAIN OF RHODOPSIN, REFINED'''
| + | Conformational changes in the phosphorylated C-terminal domain of rhodopsin during rhodopsin arrestin interactions.,Kisselev OG, Downs MA, McDowell JH, Hargrave PA J Biol Chem. 2004 Dec 3;279(49):51203-7. Epub 2004 Sep 6. PMID:15351781<ref>PMID:15351781</ref> |
| - | | + | |
| - | | + | |
| - | ==Overview==
| + | |
| - | Phosphorylation of activated G-protein-coupled receptors and the subsequent binding of arrestin mark major molecular events of homologous desensitization. In the visual system, interactions between arrestin and the phosphorylated rhodopsin are pivotal for proper termination of visual signals. By using high resolution proton nuclear magnetic resonance spectroscopy of the phosphorylated C terminus of rhodopsin, represented by a synthetic 7-phosphopolypeptide, we show that the arrestin-bound conformation is a well ordered helix-loop structure connected to rhodopsin via a flexible linker. In a model of the rhodopsin-arrestin complex, the phosphates point in the direction of arrestin and form a continuous negatively charged surface, which is stabilized by a number of positively charged lysine and arginine residues of arrestin. Opposite to the mostly extended structure of the unphosphorylated C-terminal domain of rhodopsin, the arrestin-bound C-terminal helix is a compact domain that occupies a central position between the cytoplasmic loops and occludes the key binding sites of transducin. In conjunction with other binding sites, the helix-loop structure provides a mechanism of shielding phosphates in the center of the rhodopsin-arrestin complex and appears critical in guiding arrestin for high affinity binding with rhodopsin.
| + | |
| | | | |
| - | ==About this Structure==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | 1VQX is a [[Single protein]] structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tqk 1tqk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VQX OCA].
| + | </div> |
| | + | <div class="pdbe-citations 1vqx" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Reference== | + | ==See Also== |
| - | Conformational changes in the phosphorylated C-terminal domain of rhodopsin during rhodopsin arrestin interactions., Kisselev OG, Downs MA, McDowell JH, Hargrave PA, J Biol Chem. 2004 Dec 3;279(49):51203-7. Epub 2004 Sep 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15351781 15351781]
| + | *[[Rhodopsin 3D structures|Rhodopsin 3D structures]] |
| - | [[Category: Single protein]] | + | == References == |
| - | [[Category: Downs, M A.]] | + | <references/> |
| - | [[Category: Hargrave, P A.]] | + | __TOC__ |
| - | [[Category: Kisselev, O G.]] | + | </StructureSection> |
| - | [[Category: Mcdowell, J H.]] | + | [[Category: Bos taurus]] |
| - | [[Category: Helix-loop]] | + | [[Category: Large Structures]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:48:43 2008''
| + | [[Category: Downs MA]] |
| | + | [[Category: Hargrave PA]] |
| | + | [[Category: Kisselev OG]] |
| | + | [[Category: Mcdowell JH]] |
| Structural highlights
Function
OPSD_BOVIN Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal (By similarity).[1] [2]
Publication Abstract from PubMed
Phosphorylation of activated G-protein-coupled receptors and the subsequent binding of arrestin mark major molecular events of homologous desensitization. In the visual system, interactions between arrestin and the phosphorylated rhodopsin are pivotal for proper termination of visual signals. By using high resolution proton nuclear magnetic resonance spectroscopy of the phosphorylated C terminus of rhodopsin, represented by a synthetic 7-phosphopolypeptide, we show that the arrestin-bound conformation is a well ordered helix-loop structure connected to rhodopsin via a flexible linker. In a model of the rhodopsin-arrestin complex, the phosphates point in the direction of arrestin and form a continuous negatively charged surface, which is stabilized by a number of positively charged lysine and arginine residues of arrestin. Opposite to the mostly extended structure of the unphosphorylated C-terminal domain of rhodopsin, the arrestin-bound C-terminal helix is a compact domain that occupies a central position between the cytoplasmic loops and occludes the key binding sites of transducin. In conjunction with other binding sites, the helix-loop structure provides a mechanism of shielding phosphates in the center of the rhodopsin-arrestin complex and appears critical in guiding arrestin for high affinity binding with rhodopsin.
Conformational changes in the phosphorylated C-terminal domain of rhodopsin during rhodopsin arrestin interactions.,Kisselev OG, Downs MA, McDowell JH, Hargrave PA J Biol Chem. 2004 Dec 3;279(49):51203-7. Epub 2004 Sep 6. PMID:15351781[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nakamichi H, Okada T. Local peptide movement in the photoreaction intermediate of rhodopsin. Proc Natl Acad Sci U S A. 2006 Aug 22;103(34):12729-34. Epub 2006 Aug 14. PMID:16908857
- ↑ Salom D, Lodowski DT, Stenkamp RE, Le Trong I, Golczak M, Jastrzebska B, Harris T, Ballesteros JA, Palczewski K. Crystal structure of a photoactivated deprotonated intermediate of rhodopsin. Proc Natl Acad Sci U S A. 2006 Oct 31;103(44):16123-8. Epub 2006 Oct 23. PMID:17060607
- ↑ Kisselev OG, Downs MA, McDowell JH, Hargrave PA. Conformational changes in the phosphorylated C-terminal domain of rhodopsin during rhodopsin arrestin interactions. J Biol Chem. 2004 Dec 3;279(49):51203-7. Epub 2004 Sep 6. PMID:15351781 doi:10.1074/jbc.M407341200
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