Retinoic acid receptor gamma (RAR-γ), also known as NR1B3 (nuclear receptor subfamily 1, group B, member 3) is a nuclear receptor encoded by the RARGgene.[1][2]
^Dowell P, Ishmael JE, Avram D, Peterson VJ, Nevrivy DJ, Leid M (May 1999). "Identification of nuclear receptor corepressor as a peroxisome proliferator-activated receptor alpha interacting protein". J. Biol. Chem.274 (22): 15901–7. doi:10.1074/jbc.274.22.15901. PMID10336495.
Further reading
Leid M; Kastner P; Lyons R et al. (1992). "Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently". Cell68 (2): 377–95. doi:10.1016/0092-8674(92)90478-U. PMID1310259.Cite uses deprecated parameter |author-separator= (help)
Vollberg TM; Nervi C; George MD et al. (1992). "Retinoic acid receptors as regulators of human epidermal keratinocyte differentiation". Mol. Endocrinol.6 (5): 667–76. doi:10.1210/me.6.5.667. PMID1318502.Cite uses deprecated parameter |author-separator= (help)
Mattei MG; Rivière M; Krust A et al. (1991). "Chromosomal assignment of retinoic acid receptor (RAR) genes in the human, mouse, and rat genomes". Genomics10 (4): 1061–9. doi:10.1016/0888-7543(91)90199-O. PMID1655630.Cite uses deprecated parameter |author-separator= (help)
Ishikawa T; Umesono K; Mangelsdorf DJ et al. (1990). "A functional retinoic acid receptor encoded by the gene on human chromosome 12". Mol. Endocrinol.4 (6): 837–44. doi:10.1210/mend-4-6-837. PMID2172793.Cite uses deprecated parameter |author-separator= (help)
Zitnik RJ; Kotloff RM; Latifpour J et al. (1994). "Retinoic acid inhibition of IL-1-induced IL-6 production by human lung fibroblasts". J. Immunol.152 (3): 1419–27. PMID8301142.Cite uses deprecated parameter |author-separator= (help)
Botling J; Castro DS; Oberg F et al. (1997). "Retinoic acid receptor/retinoid X receptor heterodimers can be activated through both subunits providing a basis for synergistic transactivation and cellular differentiation". J. Biol. Chem.272 (14): 9443–9. doi:10.1074/jbc.272.14.9443. PMID9083083.Cite uses deprecated parameter |author-separator= (help)
Klaholz BP; Renaud JP; Mitschler A et al. (1998). "Conformational adaptation of agonists to the human nuclear receptor RAR gamma". Nat. Struct. Biol.5 (3): 199–202. doi:10.1038/nsb0398-199. PMID9501913.Cite uses deprecated parameter |author-separator= (help)
Zhang ZP; Gambone CJ; Gabriel JL et al. (1999). "Arg278, but not Lys229 or Lys236, plays an important role in the binding of retinoic acid by retinoic acid receptor gamma". J. Biol. Chem.273 (51): 34016–21. doi:10.1074/jbc.273.51.34016. PMID9852056.Cite uses deprecated parameter |author-separator= (help)
Yang C, Zhou D, Chen S (1999). "Modulation of aromatase expression in the breast tissue by ERR alpha-1 orphan receptor". Cancer Res.58 (24): 5695–700. PMID9865725.
Nagpal S; Ghosn C; DiSepio D et al. (1999). "Retinoid-dependent recruitment of a histone H1 displacement activity by retinoic acid receptor". J. Biol. Chem.274 (32): 22563–8. doi:10.1074/jbc.274.32.22563. PMID10428834.Cite uses deprecated parameter |author-separator= (help)
Boudjelal M, Voorhees JJ, Fisher GJ (2002). "Retinoid signaling is attenuated by proteasome-mediated degradation of retinoid receptors in human keratinocyte HaCaT cells". Exp. Cell Res.274 (1): 130–7. doi:10.1006/excr.2001.5450. PMID11855864.
PDB gallery
1dsz: STRUCTURE OF THE RXR/RAR DNA-BINDING DOMAIN HETERODIMER IN COMPLEX WITH THE RETINOIC ACID RESPONSE ELEMENT DR1
1exa: ENANTIOMER DISCRIMINATION ILLUSTRATED BY CRYSTAL STRUCTURES OF THE HUMAN RETINOIC ACID RECEPTOR HRARGAMMA LIGAND BINDING DOMAIN: THE COMPLEX WITH THE ACTIVE R-ENANTIOMER BMS270394.
1exx: ENANTIOMER DISCRIMINATION ILLUSTRATED BY CRYSTAL STRUCTURES OF THE HUMAN RETINOIC ACID RECEPTOR HRARGAMMA LIGAND BINDING DOMAIN: THE COMPLEX WITH THE INACTIVE S-ENANTIOMER BMS270395.
1fcx: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID BMS184394
1fcy: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARBETA/GAMMA-SELECTIVE RETINOID CD564
1fcz: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE PANAGONIST RETINOID BMS181156
1fd0: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID SR11254
1hra: THE SOLUTION STRUCTURE OF THE HUMAN RETINOIC ACID RECEPTOR-BETA DNA-BINDING DOMAIN
2lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO ALL-TRANS RETINOIC ACID
3lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO 9-CIS RETINOIC ACID
4lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO THE SYNTHETIC AGONIST BMS961