1X7E
CRYSTAL STRUCTURE OF ESTROGEN RECEPTOR ALPHA COMPLEXED WITH WAY-244
Summary for 1X7E
| Entry DOI | 10.2210/pdb1x7e/pdb |
| Related | 1U3Q 1U3R 1U3S 1U9E 1X76 1X78 1X7B 1X7D 1X7J 1X7R |
| Descriptor | Estrogen receptor 1 (alpha), steroid receptor coactivator-3, [5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-YL]ACETONITRILE, ... (4 entities in total) |
| Functional Keywords | estrogen receptor, estrogen receptor beta, er-beta, er, estrogen receptor alpha, er-alpha, estrogen, nuclear recept transcription factor, agonist, transcription |
| Biological source | Homo sapiens (human) More |
| Cellular location | Isoform 1: Nucleus. Isoform 3: Nucleus: P03372 |
| Total number of polymer chains | 4 |
| Total formula weight | 59818.49 |
| Authors | Manas, E.S.,Unwalla, R.J.,Xu, Z.B.,Malamas, M.S.,Miller, C.P.,Harris, H.A.,Hsiao, C.,Akopian, T.,Hum, W.T.,Malakian, K.,Wolfrom, S.,Bapat, A.,Bhat, R.A.,Stahl, M.L.,Somers, W.S.,Alvarez, J.C. (deposition date: 2004-08-13, release date: 2005-03-01, Last modification date: 2024-04-03) |
| Primary citation | Manas, E.S.,Unwalla, R.J.,Xu, Z.B.,Malamas, M.S.,Miller, C.P.,Harris, H.A.,Hsiao, C.,Akopian, T.,Hum, W.T.,Malakian, K.,Wolfrom, S.,Bapat, A.,Bhat, R.A.,Stahl, M.L.,Somers, W.S.,Alvarez, J.C. Structure-Based Design of Estrogen Receptor-Beta Selective Ligands J.Am.Chem.Soc., 126:15106-15119, 2004 Cited by PubMed Abstract: We present the structure-based optimization of a series of estrogen receptor-beta (ERbeta) selective ligands. X-ray cocrystal structures of these ligands complexed to both ERalpha and ERbeta are described. We also discuss how molecular modeling was used to take advantage of subtle differences between the two binding cavities in order to optimize selectivity for ERbeta over ERalpha. Quantum chemical calculations are utilized to gain insight into the mechanism of selectivity enhancement. Despite only two relatively conservative residue substitutions in the ligand binding pocket, the most selective compounds have greater than 100-fold selectivity for ERbeta relative to ERalpha when measured using a competitive radioligand binding assay. PubMed: 15548008DOI: 10.1021/ja047633o PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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