Proteopedia

Retinoid X receptor

Revision as of 10:49, 8 August 2016 by Michal Harel (talk | contribs)

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

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Michal Harel, Alexander Berchansky, Joel L. Sussman
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