Structural highlights
Function
[ESR2_HUMAN] Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. Isoform beta-cx lacks ligand binding ability and has no or only very low ere binding activity resulting in the loss of ligand-dependent transactivation ability. DNA-binding by ESR1 and ESR2 is rapidly lost at 37 degrees Celsius in the absence of ligand while in the presence of 17 beta-estradiol and 4-hydroxy-tamoxifen loss in DNA-binding at elevated temperature is more gradual.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The syntheses of a series of 2-arylindene-1-ones as potent ligands of ERbeta and ERalpha are described. Several compounds exhibited high potency and moderate selectivity for the ERbeta receptor. X-ray and modeling studies were used to understand ligand binding orientation and observed affinity.
Estrogen receptor ligands: design and synthesis of new 2-arylindene-1-ones.,McDevitt RE, Malamas MS, Manas ES, Unwalla RJ, Xu ZB, Miller CP, Harris HA Bioorg Med Chem Lett. 2005 Jun 15;15(12):3137-42. PMID:15876535[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ McDevitt RE, Malamas MS, Manas ES, Unwalla RJ, Xu ZB, Miller CP, Harris HA. Estrogen receptor ligands: design and synthesis of new 2-arylindene-1-ones. Bioorg Med Chem Lett. 2005 Jun 15;15(12):3137-42. PMID:15876535 doi:10.1016/j.bmcl.2005.04.013
