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New page: left|200px<br /><applet load="1ln6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ln6" /> '''STRUCTURE OF BOVINE RHODOPSIN (Metarhodopsin... |
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== | ==STRUCTURE OF BOVINE RHODOPSIN (Metarhodopsin II)== | ||
The structural changes that accompany activation of a G-protein coupled | <StructureSection load='1ln6' size='340' side='right'caption='[[1ln6]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ln6]] 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=1LN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LN6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RET:RETINAL'>RET</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=1ln6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ln6 OCA], [https://pdbe.org/1ln6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ln6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ln6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ln6 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> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ln/1ln6_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ln6 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structural changes that accompany activation of a G-protein coupled receptor (GPCR) are not well understood. To better understand the activation of rhodopsin, the GPCR responsible for visual transduction, we report studies on the three-dimensional structure for the activated state of this receptor, metarhodopsin II. Differences between the three-dimensional structure of ground state rhodopsin and metarhodopsin II, particularly in the cytoplasmic face of the receptor, suggest how the receptor is activated to couple with transducin. In particular, activation opens a groove on the surface of the receptor that could bind the N-terminal helix of the G protein, transducin alpha. | |||
Structural studies of metarhodopsin II, the activated form of the G-protein coupled receptor, rhodopsin.,Choi G, Landin J, Galan JF, Birge RR, Albert AD, Yeagle PL Biochemistry. 2002 Jun 11;41(23):7318-24. PMID:12044163<ref>PMID:12044163</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ln6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Rhodopsin 3D structures|Rhodopsin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | |||
[[Category: Albert AD]] | |||
[[Category: Birge RR]] | |||
[[Category: Choi G]] | |||
[[Category: Galan JF]] | |||
[[Category: Landin J]] | |||
[[Category: Yeagle PL]] | |||
Latest revision as of 07:41, 17 October 2024
STRUCTURE OF BOVINE RHODOPSIN (Metarhodopsin II)STRUCTURE OF BOVINE RHODOPSIN (Metarhodopsin II)
Structural highlights
FunctionOPSD_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] 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 PubMedThe structural changes that accompany activation of a G-protein coupled receptor (GPCR) are not well understood. To better understand the activation of rhodopsin, the GPCR responsible for visual transduction, we report studies on the three-dimensional structure for the activated state of this receptor, metarhodopsin II. Differences between the three-dimensional structure of ground state rhodopsin and metarhodopsin II, particularly in the cytoplasmic face of the receptor, suggest how the receptor is activated to couple with transducin. In particular, activation opens a groove on the surface of the receptor that could bind the N-terminal helix of the G protein, transducin alpha. Structural studies of metarhodopsin II, the activated form of the G-protein coupled receptor, rhodopsin.,Choi G, Landin J, Galan JF, Birge RR, Albert AD, Yeagle PL Biochemistry. 2002 Jun 11;41(23):7318-24. PMID:12044163[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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