1ERE
HUMAN ESTROGEN RECEPTOR LIGAND-BINDING DOMAIN IN COMPLEX WITH 17BETA-ESTRADIOL
Summary for 1ERE
| Entry DOI | 10.2210/pdb1ere/pdb |
| Descriptor | ESTROGEN RECEPTOR, ESTRADIOL (3 entities in total) |
| Functional Keywords | nuclear receptor, transcription factor, steroid, agonist |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform 1: Nucleus. Isoform 3: Nucleus: P03372 |
| Total number of polymer chains | 6 |
| Total formula weight | 174968.42 |
| Authors | Brzozowski, A.M.,Pike, A.C.W. (deposition date: 1997-09-08, release date: 1998-09-16, Last modification date: 2024-02-07) |
| Primary citation | Brzozowski, A.M.,Pike, A.C.,Dauter, Z.,Hubbard, R.E.,Bonn, T.,Engstrom, O.,Ohman, L.,Greene, G.L.,Gustafsson, J.A.,Carlquist, M. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature, 389:753-758, 1997 Cited by PubMed Abstract: Oestrogens are involved in the growth, development and homeostasis of a number of tissues. The physiological effects of these steroids are mediated by a ligand-inducible nuclear transcription factor, the oestrogen receptor (ER). Hormone binding to the ligand-binding domain (LBD) of the ER initiates a series of molecular events culminating in the activation or repression of target genes. Transcriptional regulation arises from the direct interaction of the ER with components of the cellular transcription machinery. Here we report the crystal structures of the LBD of ER in complex with the endogenous oestrogen, 17beta-oestradiol, and the selective antagonist raloxifene, at resolutions of 3.1 and 2.6 A, respectively. The structures provide a molecular basis for the distinctive pharmacophore of the ER and its catholic binding properties. Agonist and antagonist bind at the same site within the core of the LBD but demonstrate different binding modes. In addition, each class of ligand induces a distinct conformation in the transactivation domain of the LBD, providing structural evidence of the mechanism of antagonism. PubMed: 9338790DOI: 10.1038/39645 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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