Retinoid X receptor: Difference between revisions

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<StructureSection load='1fby' size='450' side='right' caption='Structure of human retinoid X receptor α ligand-binding domain complex with 9-cis retinoic acid (PDB entry [[1fby]])' scene='51/516465/Cv/1'>
<StructureSection load='' size='350' side='right' caption='Structure of human retinoid X receptor α ligand-binding domain complex with 9-cis retinoic acid (PDB entry [[1fby]])' scene='51/516465/Cv/1'>
__TOC__
== Function ==     
== Function ==     
'''Retinoid X receptor''' (RXR) is a nuclear receptor activated by 9-''cis'' retinoic acid.  RXR makes a heterodimer with subfamily 1 nuclear receptors including retinoic acid receptor (RAR). In the absence of ligand, the RAR/RXR complex binds the hormone response elements complexed with corepressor protein.  Upon binding of the ligand, the corepressor disassociates from the receptor and associates with the coactivator leading to transcription activation.  RXR contains a DNA-binding domain (DBD) and ligand-binding domain (LBD)<ref>PMID:22020178</ref>.  For additional details on RXR-α see [[RA Mediated T-reg Differentiation]].
'''Retinoid X receptor''' (RXR) is a [[Nuclear receptors|nuclear receptor]] activated by 9-''cis'' retinoic acid.  RXR makes a heterodimer with subfamily 1 nuclear receptors including [[Retinoic acid receptor|retinoic acid receptor]] (RAR). In the absence of ligand, the RAR/RXR complex binds the hormone response elements complexed with corepressor protein.  Upon binding of the ligand, the corepressor disassociates from the receptor and associates with the coactivator leading to transcription activation.  RXR contains a DNA-binding domain (DBD) and ligand-binding domain (LBD)<ref>PMID:22020178</ref>.  For additional details on RXR-α see [[RA Mediated T-reg Differentiation]].
 
See also [[Intracellular receptors]]


There are 3 classes of RXR: α, β and γ.  <br />
There are 3 classes of RXR: α, β and γ.  <br />
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== Structural highlights ==
== Structural highlights ==
<scene name='51/516465/Cv/2'>9-''cis'' retinoid acid binds to RXRα LBD in a hydrophobic pocket</scene>. {{Template:ColorKey_Hydrophobic}},  {{Template:ColorKey_Polar}}. Water molecules shown as red spheres. <scene name='51/516465/Cv/3'>9-''cis'' retinoid acid is in a hydrophobic pocket</scene>. The ligand-binding residues are conserved in the 3 classes of RXR
<scene name='51/516465/Cv/4'>9-cis retinoid acid binds to RXRα LBD in a hydrophobic pocket</scene>. {{Template:ColorKey_Hydrophobic}},  {{Template:ColorKey_Polar}}. Water molecules are shown as red spheres. <scene name='51/516465/Cv/5'>9-cis retinoid acid is in a hydrophobic pocket</scene>. The ligand-binding residues are conserved in the 3 classes of RXR
<ref>PMID:10835357</ref>.
<ref>PMID:10835357</ref>.
</StructureSection>
==3D structures of retinoid X receptor==
==3D structures of retinoid X receptor==
[[Retinoid X receptor 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
 
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*Retinoid X receptor α
 
**[[3nsp]], [[1lbd]], [[1g1u]] - hRXR LBD – human<br />
**[[1rxr]] – hRXR DBD (mutant) – NMR<br />
**[[2q60]] – RXR LBD – ''Polyandrocarpa misakiensis''<br />
**[[1by4]] – hRXR + DNA<br />
**[[1g5y]], [[4zhs]] - hRXR LBD + retinoid<br />
**[[1dkf]] – mRXR LBD + mRAR LBD – mouse<br />
**[[1dsz]] - hRXR LBD + hRAR LBD + DNA<br />
**[[1fby]] - hRXR LBD + 9-''cis'' retinoic acid<br />
**[[3nsq]] - hRXR LBD + antagonist<br />
**[[3a9e]] - hRXR LBD + hRAR LBD + coactivator peptide<br />
**[[3fug]] - hRXR LBD + coactivator peptide<br />
**[[3fc6]] – hRXR LBD + NR1H3 protein<br />
**[[3r29]] - hRXR LBD + corepressor peptide SMRT2<br />
**[[3r2a]] - hRXR LBD + corepressor peptide SMRT2 + antagonist<br />
**[[3h0a]], [[1fm6]], [[1fm9]], [[1k74]] - hRXR LBD + PPAR-γ + 9-''cis'' retinoic acid + coactivator peptide<br />
**[[1rdt]] - hRXR LBD + PPAR-γ + coactivator peptide<br />
**[[3dzu]], [[3dzy]], [[3e00]] - hRXR LBD + PPAR-γ + 9-''cis'' retinoic acid + coactivator peptide + DNA<br />
**[[3oap]] - hRXR LBD + 9-''cis'' retinoic acid + coactivator peptide<br />
**[[3uvv]] - hRXR LBD + 9-''cis'' retinoic acid + thyronine + thyroid hormone receptor α<br />
**[[4zo1]] - hRXR LBD + coactivator peptide + thyroid hormone + thyroid hormone receptor β<br />
**[[3ozj]] - hRXR LBD + bigelovin + coactivator peptide<br />
**[[3pcu]] - hRXR LBD + rutamarin + coactivator peptide<br />
**[[2zxz]], [[2zy0]], [[3r5m]], [[1mzn]], [[1mv9]], [[1mvc]], [[4k4j]], [[4k6i]], [[4m8e]], [[4m8h]] - hRXR LBD + agonist + coactivator peptide<br />
**[[2acl]] - hRXR LBD + agonist + oxysterols receptor α<br />
**[[4ozr]], [[4ozt]] - hRXR LBD + ecdysone receptor <br />
**[[3fal]] - hRXR LBD + modulator + oxysterols receptor α + 9-''cis'' retinoic acid<br />
**[[4n5g]], [[4n8r]] - hRXR LBD + modulator <br />
**[[3kwy]] - hRXR LBD + triphenyltin + coactivator peptide<br />
**[[3e94]] - hRXR LBD + tributylin + coactivator peptide<br />
**[[2p1t]], [[2p1u]], [[2p1v]], [[4rfw]], [[4rmc]], [[4rme]], [[4rmd]] - hRXR LBD + retinoid + coactivator peptide<br />
**[[4oc7]] - hRXR LBD + acrylic acid derivative + coactivator peptide<br />
**[[5ec9]] - hRXR LBD + benzofuran derivative + coactivator peptide<br />
**[[4poh]], [[4poj]], [[4pp3]], [[4pp5]] - hRXR LBD + trienoic acid derivative + coactivator peptide<br />
**[[1xls]] - hRXR LBD (mutant) + orphan nuclear receptor NR1I3 + coactivator peptide<br />
**[[1xv9]] - hRXR LBD + orphan nuclear receptor NR1I3 + pregnane + coactivator peptide<br />
**[[1xvp]] - hRXR LBD + orphan nuclear receptor NR1I3 + CITCO + coactivator peptide<br />
**[[4j5w]] - hRXR LBD + orphan nuclear receptor PXR<br />
**[[4j5x]] - hRXR LBD + orphan nuclear receptor PXR + phosphonic acid derivative<br />
**[[4cn2]], [[4cn3]], [[4cn5]], [[4cn7]] - hRXR DBD + DNA <br />
**[[1r0n]], [[1ynw]] - hRXR DBD + DR3 response element + vitamin D3 receptor <br />
**[[4nqa]] - hRXR DBD + DR4 response element + liver X nuclear receptor + coactivator peptide <br />
 
*Retinoid X receptor β
 
**[[1xdk]] - mRXR LBD + mRAR LBD + thyroid receptor associated protein<br />
**[[1uhl]] - hRXR LBD + oxysterols receptor α + coactivator peptide<br />
**[[1h9u]] – hRXR LBD + agonist
 
*Retinoid X receptor γ


**[[2gl8]] – hRXR LBD
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 12:38, 12 January 2023

Function

Retinoid X receptor (RXR) is a nuclear receptor activated by 9-cis retinoic acid. RXR makes a heterodimer with subfamily 1 nuclear receptors including retinoic acid receptor (RAR). In the absence of ligand, the RAR/RXR complex binds the hormone response elements complexed with corepressor protein. Upon binding of the ligand, the corepressor disassociates from the receptor and associates with the coactivator leading to transcription activation. RXR contains a DNA-binding domain (DBD) and ligand-binding domain (LBD)[1]. For additional details on RXR-α see RA Mediated T-reg Differentiation.

See also Intracellular receptors

There are 3 classes of RXR: α, β and γ.

  • RXRα plays a pivotal role in liver metabolism[2].
  • RXRγ mediates the anti proliferative effects of retinoid acid.

Relevance

RXRγ is involved in working memory and despair behavior[3]. RXR pathway is a positive regulator of myelin debris clearance and has a role in age-related decline in remyelination[4].

Structural highlights

. Hydrophobic, Polar. Water molecules are shown as red spheres. . The ligand-binding residues are conserved in the 3 classes of RXR

[5].

3D structures of retinoid X receptor

Retinoid X receptor 3D structures


Structure of human retinoid X receptor α ligand-binding domain complex with 9-cis retinoic acid (PDB entry 1fby)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Dawson MI, Xia Z. The retinoid X receptors and their ligands. Biochim Biophys Acta. 2012 Jan;1821(1):21-56. doi: 10.1016/j.bbalip.2011.09.014. , Epub 2011 Oct 1. PMID:22020178 doi:http://dx.doi.org/10.1016/j.bbalip.2011.09.014
  2. ↑ Wu Y, Zhang X, Bardag-Gorce F, Robel RC, Aguilo J, Chen L, Zeng Y, Hwang K, French SW, Lu SC, Wan YJ. Retinoid X receptor alpha regulates glutathione homeostasis and xenobiotic detoxification processes in mouse liver. Mol Pharmacol. 2004 Mar;65(3):550-7. PMID:14978233 doi:http://dx.doi.org/10.1124/mol.65.3.550
  3. ↑ Wietrzych-Schindler M, Szyszka-Niagolov M, Ohta K, Endo Y, Perez E, de Lera AR, Chambon P, Krezel W. Retinoid x receptor gamma is implicated in docosahexaenoic acid modulation of despair behaviors and working memory in mice. Biol Psychiatry. 2011 Apr 15;69(8):788-94. doi: 10.1016/j.biopsych.2010.12.017., Epub 2011 Feb 21. PMID:21334601 doi:http://dx.doi.org/10.1016/j.biopsych.2010.12.017
  4. ↑ Natrajan MS, de la Fuente AG, Crawford AH, Linehan E, Nunez V, Johnson KR, Wu T, Fitzgerald DC, Ricote M, Bielekova B, Franklin RJ. Retinoid X receptor activation reverses age-related deficiencies in myelin debris phagocytosis and remyelination. Brain. 2015 Dec;138(Pt 12):3581-97. doi: 10.1093/brain/awv289. Epub 2015 Oct 12. PMID:26463675 doi:http://dx.doi.org/10.1093/brain/awv289
  5. ↑ Egea PF, Mitschler A, Rochel N, Ruff M, Chambon P, Moras D. Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid. EMBO J. 2000 Jun 1;19(11):2592-601. PMID:10835357 doi:10.1093/emboj/19.11.2592

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Michal Harel, Alexander Berchansky, Joel L. Sussman
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