2x72: Difference between revisions

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-[[Image:2x72.png|left|200px]]
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+==CRYSTAL STRUCTURE OF THE CONSTITUTIVELY ACTIVE E113Q,D2C,D282C RHODOPSIN MUTANT WITH BOUND GALPHACT PEPTIDE.==
-The line below this paragraph, containing "STRUCTURE_2x72", creates the "Structure Box" on the page.
+<StructureSection load='2x72' size='340' side='right'caption='[[2x72]], [[Resolution|resolution]] 3.00&Aring;' 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'>[[2x72]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X72 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">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=LPP:2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL+HEXADECANOATE'>LPP</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEF:DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE'>PEF</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr>
-{{STRUCTURE_2x72|  PDB=2x72  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2x72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x72 OCA], [https://pdbe.org/2x72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x72 RCSB], [https://www.ebi.ac.uk/pdbsum/2x72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x72 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 ==
+G-protein-coupled receptors (GPCRs) comprise the largest family of membrane proteins in the human genome and mediate cellular responses to an extensive array of hormones, neurotransmitters and sensory stimuli. Although some crystal structures have been determined for GPCRs, most are for modified forms, showing little basal activity, and are bound to inverse agonists or antagonists. Consequently, these structures correspond to receptors in their inactive states. The visual pigment rhodopsin is the only GPCR for which structures exist that are thought to be in the active state. However, these structures are for the apoprotein, or opsin, form that does not contain the agonist all-trans retinal. Here we present a crystal structure at a resolution of 3 A for the constitutively active rhodopsin mutant Glu 113 Gln in complex with a peptide derived from the carboxy terminus of the alpha-subunit of the G protein transducin. The protein is in an active conformation that retains retinal in the binding pocket after photoactivation. Comparison with the structure of ground-state rhodopsin suggests how translocation of the retinal beta-ionone ring leads to a rotation of transmembrane helix 6, which is the critical conformational change on activation. A key feature of this conformational change is a reorganization of water-mediated hydrogen-bond networks between the retinal-binding pocket and three of the most conserved GPCR sequence motifs. We thus show how an agonist ligand can activate its GPCR.
-===CRYSTAL STRUCTURE OF THE CONSTITUTIVELY ACTIVE E113Q,N2C, D282C RHODOPSIN MUTANT WITH BOUND GALPHACT PEPTIDE.===
+The structural basis of agonist-induced activation in constitutively active rhodopsin.,Standfuss J, Edwards PC, D'Antona A, Fransen M, Xie G, Oprian DD, Schertler GF Nature. 2011 Mar 31;471(7340):656-60. Epub 2011 Mar 9. PMID:21389983<ref>PMID:21389983</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_21389983}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2x72" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 21389983 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_21389983}}
-==About this Structure==
-[[2x72]] is a 2 chain structure of [[Rhodopsin]] with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X72 OCA].
 ==See Also==
-*[[Rhodopsin]]
+*[[Rhodopsin 3D structures|Rhodopsin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:021389983</ref><ref group="xtra">PMID:017825322</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Bos taurus]]
-[[Category: Dantona, A.]]
+[[Category: Large Structures]]
-[[Category: Edwards, P C.]]
+[[Category: Dantona A]]
-[[Category: Fransen, M.]]
+[[Category: Edwards PC]]
-[[Category: Oprian, D D.]]
+[[Category: Fransen M]]
-[[Category: Schertler, G F.X.]]
+[[Category: Oprian DD]]
-[[Category: Standfuss, J.]]
+[[Category: Schertler GFX]]
-[[Category: Xie, G.]]
+[[Category: Standfuss J]]
-[[Category: Chromophore]]
+[[Category: Xie G]]
-[[Category: G-protein coupled receptor]]
-[[Category: Glycoprotein]]
-[[Category: Lipoprotein]]
-[[Category: Photoreceptor protein]]
-[[Category: Retinal protein]]
-[[Category: Sensory transduction]]
-[[Category: Signaling protein]]
-[[Category: Transmembrane]]