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1ere
From Proteopedia
Contents |
HUMAN ESTROGEN RECEPTOR LIGAND-BINDING DOMAIN IN COMPLEX WITH 17BETA-ESTRADIOL
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.
Molecular basis of agonism and antagonism in the oestrogen receptor., Brzozowski AM, Pike AC, Dauter Z, Hubbard RE, Bonn T, Engstrom O, Ohman L, Greene GL, Gustafsson JA, Carlquist M, Nature. 1997 Oct 16;389(6652):753-8. PMID:9338790
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1ere is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Brzozowski AM, Pike AC, Dauter Z, Hubbard RE, Bonn T, Engstrom O, Ohman L, Greene GL, Gustafsson JA, Carlquist M. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature. 1997 Oct 16;389(6652):753-8. PMID:9338790 doi:10.1038/39645
- Pike AC, Brzozowski AM, Walton J, Hubbard RE, Thorsell AG, Li YL, Gustafsson JA, Carlquist M. Structural insights into the mode of action of a pure antiestrogen. Structure. 2001 Feb 7;9(2):145-53. PMID:11250199
