3fal: Difference between revisions

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 ==humanRXR alpha & mouse LXR alpha complexed with Retenoic acid and GSK2186==
-<StructureSection load='3fal' size='340' side='right' caption='[[3fal]], [[Resolution|resolution]] 2.36&Aring;' scene=''>
+<StructureSection load='3fal' size='340' side='right'caption='[[3fal]], [[Resolution|resolution]] 2.36&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3fal]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FAL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FAL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3fal]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FAL FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LO2:2-{4-[BUTYL(3-CHLORO-4,5-DIMETHOXYBENZYL)AMINO]PHENYL}-1,1,1,3,3,3-HEXAFLUOROPROPAN-2-OL'>LO2</scene>, <scene name='pdbligand=REA:RETINOIC+ACID'>REA</scene><br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.36&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RXRA, NR2B1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), Nr1h3, Lxra ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LO2:2-{4-[BUTYL(3-CHLORO-4,5-DIMETHOXYBENZYL)AMINO]PHENYL}-1,1,1,3,3,3-HEXAFLUOROPROPAN-2-OL'>LO2</scene>, <scene name='pdbligand=REA:RETINOIC+ACID'>REA</scene></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3fal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fal OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fal RCSB], [http://www.ebi.ac.uk/pdbsum/3fal PDBsum]</span></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=3fal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fal OCA], [https://pdbe.org/3fal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fal RCSB], [https://www.ebi.ac.uk/pdbsum/3fal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fal ProSAT]</span></td></tr>
-<table>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/RXRA_HUMAN RXRA_HUMAN] Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a common heterodimeric partner for a number of nuclear receptors. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes.<ref>PMID:10195690</ref> <ref>PMID:11162439</ref> <ref>PMID:11915042</ref> <ref>PMID:20215566</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/fa/3fal_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fa/3fal_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=3fal ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3fal" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Retinoid X receptor|Retinoid X receptor]]
+*[[Liver X receptor|Liver X receptor]]
+*[[Retinoid X receptor 3D structures|Retinoid X receptor 3D structures]]
 == References ==
 <references/>
@@ Line 33: / Line 38: @@
 </StructureSection>
 [[Category: Homo sapiens]]
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Billin, A N.]]
+[[Category: Billin AN]]
-[[Category: Campobasso, N.]]
+[[Category: Campobasso N]]
-[[Category: Caravella, J A.]]
+[[Category: Caravella JA]]
-[[Category: Chao, E Y.]]
+[[Category: Chao EY]]
-[[Category: Collins, J L.]]
+[[Category: Collins JL]]
-[[Category: Galardi, C.]]
+[[Category: Galardi C]]
-[[Category: Ghisletti, S.]]
+[[Category: Ghisletti S]]
-[[Category: Watson, M A.]]
+[[Category: Watson MA]]
-[[Category: Willson, T M.]]
+[[Category: Willson TM]]
-[[Category: Zuercher, W J.]]
+[[Category: Zuercher WJ]]
-[[Category: Dna-binding]]
-[[Category: Host-virus interaction]]
-[[Category: Metal-binding]]
-[[Category: Nuclear hormone receptor nonsteroidal lxr agonist choloestorol metabolism]]
-[[Category: Nucleus]]
-[[Category: Receptor]]
-[[Category: Signaling protein]]
-[[Category: Transcription]]
-[[Category: Transcription regulation]]
-[[Category: Zinc-finger]]