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". The Journal of Biological Chemistry. 274 (22): 15901–7. doi:10.1074/jbc.274.22.15901. PMID10336495.
Further reading
Leid M, Kastner P, Lyons R, Nakshatri H, Saunders M, Zacharewski T, Chen JY, Staub A, Garnier JM, Mader S (Jan 1992). "Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently". Cell. 68 (2): 377–95. doi:10.1016/0092-8674(92)90478-U. PMID1310259.
Vollberg TM, Nervi C, George MD, Fujimoto W, Krust A, Jetten AM (May 1992). "Retinoic acid receptors as regulators of human epidermal keratinocyte differentiation". Molecular Endocrinology. 6 (5): 667–76. doi:10.1210/me.6.5.667. PMID1318502.
Mattei MG, Rivière M, Krust A, Ingvarsson S, Vennström B, Islam MQ, Levan G, Kautner P, Zelent A, Chambon P (Aug 1991). "Chromosomal assignment of retinoic acid receptor (RAR) genes in the human, mouse, and rat genomes". Genomics. 10 (4): 1061–9. doi:10.1016/0888-7543(91)90199-O. PMID1655630.
Ishikawa T, Umesono K, Mangelsdorf DJ, Aburatani H, Stanger BZ, Shibasaki Y, Imawari M, Evans RM, Takaku F (Jun 1990). "A functional retinoic acid receptor encoded by the gene on human chromosome 12". Molecular Endocrinology. 4 (6): 837–44. doi:10.1210/mend-4-6-837. PMID2172793.
Zitnik RJ, Kotloff RM, Latifpour J, Zheng T, Whiting NL, Schwalb J, Elias JA (Feb 1994). "Retinoic acid inhibition of IL-1-induced IL-6 production by human lung fibroblasts". Journal of Immunology. 152 (3): 1419–27. PMID8301142.
Botling J, Castro DS, Oberg F, Nilsson K, Perlmann T (Apr 1997). "Retinoic acid receptor/retinoid X receptor heterodimers can be activated through both subunits providing a basis for synergistic transactivation and cellular differentiation". The Journal of Biological Chemistry. 272 (14): 9443–9. doi:10.1074/jbc.272.14.9443. PMID9083083.
Lømo J, Smeland EB, Ulven S, Natarajan V, Blomhoff R, Gandhi U, Dawson MI, Blomhoff HK (Apr 1998). "RAR-, not RXR, ligands inhibit cell activation and prevent apoptosis in B-lymphocytes". Journal of Cellular Physiology. 175 (1): 68–77. doi:10.1002/(SICI)1097-4652(199804)175:1<68::AID-JCP8>3.0.CO;2-A. PMID9491782.
Klaholz BP, Renaud JP, Mitschler A, Zusi C, Chambon P, Gronemeyer H, Moras D (Mar 1998). "Conformational adaptation of agonists to the human nuclear receptor RAR gamma". Nature Structural Biology. 5 (3): 199–202. doi:10.1038/nsb0398-199. PMID9501913.
Zhang ZP, Gambone CJ, Gabriel JL, Wolfgang CL, Soprano KJ, Soprano DR (Dec 1998). "Arg278, but not Lys229 or Lys236, plays an important role in the binding of retinoic acid by retinoic acid receptor gamma". The Journal of Biological Chemistry. 273 (51): 34016–21. doi:10.1074/jbc.273.51.34016. PMID9852056.
Yang C, Zhou D, Chen S (Dec 1998). "Modulation of aromatase expression in the breast tissue by ERR alpha-1 orphan receptor". Cancer Research. 58 (24): 5695–700. PMID9865725.
Nagpal S, Ghosn C, DiSepio D, Molina Y, Sutter M, Klein ES, Chandraratna RA (Aug 1999). "Retinoid-dependent recruitment of a histone H1 displacement activity by retinoic acid receptor". The Journal of Biological Chemistry. 274 (32): 22563–8. doi:10.1074/jbc.274.32.22563. PMID10428834.
1dsz: STRUCTURE OF THE RXR/RAR DNA-BINDING DOMAIN HETERODIMER IN COMPLEX WITH THE RETINOIC ACID RESPONSE ELEMENT DR1
PDB 1exa EBI.jpg
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.
PDB 1exx EBI.jpg
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.
PDB 1fcx EBI.jpg
1fcx: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID BMS184394
PDB 1fcy EBI.jpg
1fcy: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARBETA/GAMMA-SELECTIVE RETINOID CD564
PDB 1fcz EBI.jpg
1fcz: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE PANAGONIST RETINOID BMS181156
PDB 1fd0 EBI.jpg
1fd0: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID SR11254
PDB 1hra EBI.jpg
1hra: THE SOLUTION STRUCTURE OF THE HUMAN RETINOIC ACID RECEPTOR-BETA DNA-BINDING DOMAIN
PDB 2lbd EBI.jpg
2lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO ALL-TRANS RETINOIC ACID
PDB 3lbd EBI.jpg
3lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO 9-CIS RETINOIC ACID
PDB 4lbd EBI.jpg
4lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO THE SYNTHETIC AGONIST BMS961