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Human Estrogen Receptor Alpha Ligand-binding Domain in Complex with the Antagonist Ligand 4-DHuman Estrogen Receptor Alpha Ligand-binding Domain in Complex with the Antagonist Ligand 4-D
Structural highlights
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 PubMedThe discovery and synthesis of dihydrobenzoxathiins as potent, ERalpha subtype selective ligands are described. The most active analogue, 4-D, was found to be 50-fold selective in a competitive binding assay and 100-fold selective in a transactivation assay in HEK-293 cells. The alpha selectivity was postulated to lie in the interaction of the sulfur atom of the benzoxathiin ring with the two discriminating residues in the binding pocket of the receptor isoforms. Estrogen receptor ligands. II. Discovery of benzoxathiins as potent, selective estrogen receptor alpha modulators.,Kim S, Wu JY, Birzin ET, Frisch K, Chan W, Pai LY, Yang YT, Mosley RT, Fitzgerald PM, Sharma N, Dahllund J, Thorsell AG, DiNinno F, Rohrer SP, Schaeffer JM, Hammond ML J Med Chem. 2004 Apr 22;47(9):2171-5. PMID:15084115[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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