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| | ==NMR structures of phosphorylated carboxy terminus of bovine rhodopsin in arrestin-bound state== | | ==NMR structures of phosphorylated carboxy terminus of bovine rhodopsin in arrestin-bound state== |
| - | <StructureSection load='1nzs' size='340' side='right'caption='[[1nzs]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''> | + | <StructureSection load='1nzs' size='340' side='right'caption='[[1nzs]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1nzs]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NZS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NZS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1nzs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NZS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NZS FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | + | </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='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=1nzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nzs OCA], [http://pdbe.org/1nzs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nzs RCSB], [http://www.ebi.ac.uk/pdbsum/1nzs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nzs ProSAT]</span></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> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nzs OCA], [https://pdbe.org/1nzs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nzs RCSB], [https://www.ebi.ac.uk/pdbsum/1nzs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nzs ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Rhodopsin|Rhodopsin]] | + | *[[Rhodopsin 3D structures|Rhodopsin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hargrave, P A]] | + | [[Category: Hargrave PA]] |
| - | [[Category: Kisselev, O G]] | + | [[Category: Kisselev OG]] |
| - | [[Category: McDowell, J H]] | + | [[Category: McDowell JH]] |
| - | [[Category: Arrestin]]
| + | |
| - | [[Category: Ball-and-chain]]
| + | |
| - | [[Category: Bound conformation]]
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| - | [[Category: Gpcr]]
| + | |
| - | [[Category: Helix-loop]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Rhodopsin]]
| + | |
| - | [[Category: Signal termination]]
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| - | [[Category: Signaling protein]]
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| 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
Visual arrestin binds to the phosphorylated carboxy-terminal region of rhodopsin to block interactions with transducin and terminate signaling in the rod photoreceptor cells. A synthetic seven-phospho-peptide from the C-terminal region of rhodopsin, Rh(330-348), has been shown to bind arrestin and mimic inhibition of signal transduction. In this study, we examine conformational changes in this synthetic peptide upon binding to arrestin by high-resolution proton nuclear magnetic resonance (NMR). We show that the peptide is completely disordered in solution, but becomes structured upon binding to arrestin. A control, unphosphorylated peptide that fails to bind to arrestin remains highly disordered. Specific NMR distance constraints are used to model the arrestin-bound conformation. The models suggest that the phosphorylated carboxy-terminal region of rhodopsin, Rh(330-348), undergoes significant conformational changes and becomes structured upon binding to arrestin.
The arrestin-bound conformation and dynamics of the phosphorylated carboxy-terminal region of rhodopsin.,Kisselev OG, McDowell JH, Hargrave PA FEBS Lett. 2004 Apr 30;564(3):307-11. PMID:15111114[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, McDowell JH, Hargrave PA. The arrestin-bound conformation and dynamics of the phosphorylated carboxy-terminal region of rhodopsin. FEBS Lett. 2004 Apr 30;564(3):307-11. PMID:15111114 doi:10.1016/S0014-5793(04)00226-1
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