Retinoid X receptor: Difference between revisions

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<StructureSection load='1g5y' size='350' side='right' caption='Structure of human retinoid X receptor ligand-binding domain tetramer complex with retinoid  (PDB entry [[1g5y]])' scene=''>
<StructureSection load='1g5y' size='350' side='right' caption='Structure of human retinoid X receptor α ligand-binding domain tetramer complex with retinoid  (PDB entry [[1g5y]])' scene=''>
   
== 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.  RAR contains a DNA-binding domain (DBD) and ligand-binding domain (LBD).  There are 3 classes of RXR: α, β and γ.  For additional details on RXR-α see [[RA Mediated T-reg Differentiation]].
'''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]].
 
There are 3 classes of RXR: α, β and γ.  <br />
*'''RXRα''' plays a pivotal role in liver metabolism<ref>PMID:14978233</ref>.<br />
*'''RXRγ''' mediates the anti proliferative effects of retinoid acid.<br />
 
== Relevance ==
*RXRγ is involved in working memory and despair behavior<ref>PMID:21334601</ref>.<br />
 
== Structural highlights ==
 
<ref>PMID:12906827</ref>
</StructureSection>
</StructureSection>


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**[[1dkf]] – mRXR LBD + mRAR LBD – mouse<br />
**[[1dkf]] – mRXR LBD + mRAR LBD – mouse<br />
**[[1dsz]] - hRXR LBD + hRAR LBD + DNA<br />
**[[1dsz]] - hRXR LBD + hRAR LBD + DNA<br />
**[[1fby]] - hRXR LBD + 9-cis retinoic acid<br />
**[[1fby]] - hRXR LBD + 9-''cis'' retinoic acid<br />
**[[3nsq]] - hRXR LBD + antagonist<br />
**[[3nsq]] - hRXR LBD + antagonist<br />
**[[3a9e]] - hRXR LBD + hRAR LBD + coactivator peptide<br />
**[[3a9e]] - hRXR LBD + hRAR LBD + coactivator peptide<br />
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**[[3r29]] - hRXR LBD + corepressor peptide SMRT2<br />
**[[3r29]] - hRXR LBD + corepressor peptide SMRT2<br />
**[[3r2a]] - hRXR LBD + corepressor peptide SMRT2 + antagonist<br />
**[[3r2a]] - hRXR LBD + corepressor peptide SMRT2 + antagonist<br />
**[[3h0a]], [[1fm6]], [[1fm9]], [[1k74]] - hRXR LBD + PPAR-γ + 9-cis retinoic acid + coactivator peptide<br />
**[[3h0a]], [[1fm6]], [[1fm9]], [[1k74]] - hRXR LBD + PPAR-γ + 9-''cis'' retinoic acid + coactivator peptide<br />
**[[1rdt]] - hRXR LBD + PPAR-γ + 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 />
**[[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 />
**[[3oap]] - hRXR LBD + 9-''cis'' retinoic acid + coactivator peptide<br />
**[[3uvv]] - hRXR LBD + 9-cis retinoic acid + thyronine + thyroid hormone receptor α<br />
**[[3uvv]] - hRXR LBD + 9-''cis'' retinoic acid + thyronine + thyroid hormone receptor α<br />
**[[3ozj]] - hRXR LBD + bigelovin + coactivator peptide<br />
**[[3ozj]] - hRXR LBD + bigelovin + coactivator peptide<br />
**[[3pcu]] - hRXR LBD + rutamarin + coactivator peptide<br />
**[[3pcu]] - hRXR LBD + rutamarin + coactivator peptide<br />
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**[[2acl]] - hRXR LBD + agonist + oxysterols receptor α<br />
**[[2acl]] - hRXR LBD + agonist + oxysterols receptor α<br />
**[[4ozr]], [[4ozt]] - hRXR LBD + ecdysone receptor <br />
**[[4ozr]], [[4ozt]] - hRXR LBD + ecdysone receptor <br />
**[[3fal]] - hRXR LBD + modulator + oxysterols receptor α + 9-cis retinoic acid<br />
**[[3fal]] - hRXR LBD + modulator + oxysterols receptor α + 9-''cis'' retinoic acid<br />
**[[4n5g]], [[4n8r]] - hRXR LBD + modulator <br />
**[[4n5g]], [[4n8r]] - hRXR LBD + modulator <br />
**[[3kwy]] - hRXR LBD + triphenyltin + coactivator peptide<br />
**[[3kwy]] - hRXR LBD + triphenyltin + coactivator peptide<br />
Line 62: Line 73:
**[[2gl8]] – hRXR LBD
**[[2gl8]] – hRXR LBD
}}
}}
== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 10:49, 8 August 2016

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.

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].

Structural highlights

[4]

Structure of human retinoid X receptor α ligand-binding domain tetramer complex with retinoid (PDB entry 1g5y)

Drag the structure with the mouse to rotate

3D structures of retinoid X receptor3D structures of retinoid X receptor

Updated on 08-August-2016

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. ↑ Ireton GC, Black ME, Stoddard BL. The 1.14 A crystal structure of yeast cytosine deaminase: evolution of nucleotide salvage enzymes and implications for genetic chemotherapy. Structure. 2003 Aug;11(8):961-72. PMID:12906827

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

Michal Harel, Alexander Berchansky, Joel L. Sussman
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