| First Author | Sogawa K | Year | 1997 |
| Journal | J Biochem | Volume | 122 |
| Issue | 6 | Pages | 1075-9 |
| PubMed ID | 9498548 | Mgi Jnum | J:44972 |
| Mgi Id | MGI:1101550 | Doi | 10.1093/oxfordjournals.jbchem.a021864 |
| Citation | Sogawa K, et al. (1997) Ah receptor, a novel ligand-activated transcription factor. J Biochem 122(6):1075-9 |
| abstractText | The aryl hydrocarbon receptor (AhR) is widely distributed in vertebrates and is known to be involved in metabolism of xenobiotics including man-made chemicals, most of which act as a ligand for the receptor, although no endogeneous ligand has yet been known. Upon binding a ligand, the receptor is activated to translocate to the nuclei, and during the nuclear translocation process, it is dissociated from the 90 kDa heat shock protein (Hsp90) to form a heterodimer with Arnt (Ah receptor nuclear translocator). The heterodimer complex binds a DNA response element termed xenobiotic responsive element (XRE) localized upstream of the target genes of many drug-metabolizing enzymes including cytochrome P4501A1 and glutathione S-transferase to activate their transcription. Recent cDNA cloning has revealed that the AhR, like Arnt, possesses characteristic structural motifs of basic helix-loop-helix and PAS domains responsible for DNA recognition, heterodimerization, and ligand binding, and functions as a novel receptor-type transcription factor. |
