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==Human Retinoic acid receptor RXR-gamma ligand-binding domain== | ==Human Retinoic acid receptor RXR-gamma ligand-binding domain== | ||
<StructureSection load='2gl8' size='340' side='right' caption='[[2gl8]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2gl8' size='340' side='right'caption='[[2gl8]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2gl8]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2gl8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GL8 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RXRG, NR2B3 ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RXRG, NR2B3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gl8 OCA], [https://pdbe.org/2gl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gl8 RCSB], [https://www.ebi.ac.uk/pdbsum/2gl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gl8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/RXRG_HUMAN RXRG_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 (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 21: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Retinoid X receptor|Retinoid X receptor]] | *[[Retinoid X receptor 3D structures|Retinoid X receptor 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
[[Category: Bochkarev, A]] | [[Category: Bochkarev, A]] | ||
Revision as of 22:08, 10 March 2021
Human Retinoic acid receptor RXR-gamma ligand-binding domainHuman Retinoic acid receptor RXR-gamma ligand-binding domain
Structural highlights
Function[RXRG_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 (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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