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| - | [[Image:1fdf.gif|left|200px]]<br /><applet load="1fdf" size="450" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="1fdf" /> | |
| - | '''HELIX 7 BOVINE RHODOPSIN'''<br /> | |
| | | | |
| - | ==Overview== | + | ==HELIX 7 BOVINE RHODOPSIN== |
| - | PURPOSE: The three dimensional structure of a peptide comprising the, sequence of the seventh transmembrane segment of the G-protein coupled, receptor, rhodopsin, was determined in solution. METHODS: The sequence of, the seventh transmembrane segment of rhodopsin, which contains the NPxxY, sequence that is highly conserved among G-protein coupled receptors and, lys296 that forms the Schiff base with the retinal, was synthesized by, solid phase peptide synthesis. The three dimensional structure was, determined in solution by high-resolution nuclear magnetic resonance, (NMR). RESULTS: The structure revealed a helix-break-helix motif for this, sequence. Two families of structures were observed which differed in the, angle between the two helical segments. The sequence of this transmembrane, segment overlapped significantly the sequence of a peptide from the, carboxyl terminal of rhodopsin, the structure of which was solved, previously. The redundant sequence formed a helix in both peptides. It was, therefore possible to superimpose the redundant sequence of both peptides, and construct a structure for rhodopsin encompassing residues 291-348., CONCLUSIONS: This structure reveals locations of the lys296 and the, acylation sites of rhodopsin that are consistent with the known, biochemistry of this receptor. This segmentation approach to membrane, protein structure provides important structural information in the absence, of an X-ray crystal structure of rhodopsin. The approach is expected to be, useful for other G-protein coupled receptors. | + | <StructureSection load='1fdf' size='340' side='right'caption='[[1fdf]]' scene=''> |
| | + | == Structural highlights == |
| | + | <table><tr><td colspan='2'>[[1fdf]] 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=1FDF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FDF FirstGlance]. <br> |
| | + | </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'>[https://proteopedia.org/fgij/fg.htm?mol=1fdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdf OCA], [https://pdbe.org/1fdf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fdf RCSB], [https://www.ebi.ac.uk/pdbsum/1fdf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fdf 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 == |
| | + | PURPOSE: The three dimensional structure of a peptide comprising the sequence of the seventh transmembrane segment of the G-protein coupled receptor, rhodopsin, was determined in solution. METHODS: The sequence of the seventh transmembrane segment of rhodopsin, which contains the NPxxY sequence that is highly conserved among G-protein coupled receptors and lys296 that forms the Schiff base with the retinal, was synthesized by solid phase peptide synthesis. The three dimensional structure was determined in solution by high-resolution nuclear magnetic resonance (NMR). RESULTS: The structure revealed a helix-break-helix motif for this sequence. Two families of structures were observed which differed in the angle between the two helical segments. The sequence of this transmembrane segment overlapped significantly the sequence of a peptide from the carboxyl terminal of rhodopsin, the structure of which was solved previously. The redundant sequence formed a helix in both peptides. It was therefore possible to superimpose the redundant sequence of both peptides and construct a structure for rhodopsin encompassing residues 291-348. CONCLUSIONS: This structure reveals locations of the lys296 and the acylation sites of rhodopsin that are consistent with the known biochemistry of this receptor. This segmentation approach to membrane protein structure provides important structural information in the absence of an X-ray crystal structure of rhodopsin. The approach is expected to be useful for other G-protein coupled receptors. |
| | | | |
| - | ==About this Structure==
| + | Three dimensional structure of the seventh transmembrane helical domain of the G-protein receptor, rhodopsin.,Yeagle PL, Danis C, Choi G, Alderfer JL, Albert AD Mol Vis. 2000 Jul 27;6:125-31. PMID:10930473<ref>PMID:10930473</ref> |
| - | 1FDF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FDF OCA].
| + | |
| | | | |
| - | ==Reference==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | Three dimensional structure of the seventh transmembrane helical domain of the G-protein receptor, rhodopsin., Yeagle PL, Danis C, Choi G, Alderfer JL, Albert AD, Mol Vis. 2000 Jul 27;6:125-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10930473 10930473]
| + | </div> |
| - | [[Category: Single protein]]
| + | <div class="pdbe-citations 1fdf" style="background-color:#fffaf0;"></div> |
| - | [[Category: Albert, A.D.]]
| + | |
| - | [[Category: Alderfer, J.L.]]
| + | |
| - | [[Category: Choi, G.]]
| + | |
| - | [[Category: Danis, C.]]
| + | |
| - | [[Category: Yeagle, P.L.]]
| + | |
| - | [[Category: helix]]
| + | |
| | | | |
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:50:16 2007''
| + | ==See Also== |
| | + | *[[Rhodopsin 3D structures|Rhodopsin 3D structures]] |
| | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | + | [[Category: Bos taurus]] |
| | + | [[Category: Large Structures]] |
| | + | [[Category: Albert AD]] |
| | + | [[Category: Alderfer JL]] |
| | + | [[Category: Choi G]] |
| | + | [[Category: Danis C]] |
| | + | [[Category: Yeagle PL]] |
| 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
PURPOSE: The three dimensional structure of a peptide comprising the sequence of the seventh transmembrane segment of the G-protein coupled receptor, rhodopsin, was determined in solution. METHODS: The sequence of the seventh transmembrane segment of rhodopsin, which contains the NPxxY sequence that is highly conserved among G-protein coupled receptors and lys296 that forms the Schiff base with the retinal, was synthesized by solid phase peptide synthesis. The three dimensional structure was determined in solution by high-resolution nuclear magnetic resonance (NMR). RESULTS: The structure revealed a helix-break-helix motif for this sequence. Two families of structures were observed which differed in the angle between the two helical segments. The sequence of this transmembrane segment overlapped significantly the sequence of a peptide from the carboxyl terminal of rhodopsin, the structure of which was solved previously. The redundant sequence formed a helix in both peptides. It was therefore possible to superimpose the redundant sequence of both peptides and construct a structure for rhodopsin encompassing residues 291-348. CONCLUSIONS: This structure reveals locations of the lys296 and the acylation sites of rhodopsin that are consistent with the known biochemistry of this receptor. This segmentation approach to membrane protein structure provides important structural information in the absence of an X-ray crystal structure of rhodopsin. The approach is expected to be useful for other G-protein coupled receptors.
Three dimensional structure of the seventh transmembrane helical domain of the G-protein receptor, rhodopsin.,Yeagle PL, Danis C, Choi G, Alderfer JL, Albert AD Mol Vis. 2000 Jul 27;6:125-31. PMID:10930473[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
- ↑ Yeagle PL, Danis C, Choi G, Alderfer JL, Albert AD. Three dimensional structure of the seventh transmembrane helical domain of the G-protein receptor, rhodopsin. Mol Vis. 2000 Jul 27;6:125-31. PMID:10930473
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