3fal: Difference between revisions

No edit summary
No edit summary
 
(2 intermediate revisions by the same user not shown)
Line 1: Line 1:


==humanRXR alpha & mouse LXR alpha complexed with Retenoic acid and GSK2186==
==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 ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3fal]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 id='ligand'><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></td></tr>
</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 id='gene'><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 HUMAN]), Nr1h3, Lxra ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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 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=3fal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fal OCA], [http://pdbe.org/3fal PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fal RCSB], [http://www.ebi.ac.uk/pdbsum/3fal PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fal ProSAT]</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 ==
== Function ==
[[http://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> [[http://www.uniprot.org/uniprot/NR1H3_MOUSE NR1H3_MOUSE]] Orphan receptor. Interaction with RXR shifts RXR from its role as a silent DNA-binding partner to an active ligand-binding subunit in mediating retinoid responses through target genes defined by LXRES. LXRES are DR4-type response elements characterized by direct repeats of two similar hexanuclotide half-sites spaced by four nucleotides. Plays an important role in the regulation of cholesterol homeostasis, regulating cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8.<ref>PMID:19520913</ref> <ref>PMID:20427281</ref> 
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <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>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 31: Line 31:


==See Also==
==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 ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Lk3 transgenic mice]]
[[Category: Large Structures]]
[[Category: Billin, A N]]
[[Category: Mus musculus]]
[[Category: Campobasso, N]]
[[Category: Billin AN]]
[[Category: Caravella, J A]]
[[Category: Campobasso N]]
[[Category: Chao, E Y]]
[[Category: Caravella JA]]
[[Category: Collins, J L]]
[[Category: Chao EY]]
[[Category: Galardi, C]]
[[Category: Collins JL]]
[[Category: Ghisletti, S]]
[[Category: Galardi C]]
[[Category: Watson, M A]]
[[Category: Ghisletti S]]
[[Category: Willson, T M]]
[[Category: Watson MA]]
[[Category: Zuercher, W J]]
[[Category: Willson TM]]
[[Category: Dna-binding]]
[[Category: Zuercher WJ]]
[[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]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA