A structural biologist's view of the oestrogen receptor.
Here we review the results that have emerged from our structural studies on the oestrogen receptor ligand-binding domain (ER-LBD). The effects of agonists and antagonists on the structure of ERalpha- and ERbeta-LBDs are examined. In addition, the findings from structural studies of ER-LBD in complex...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
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2000
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| _version_ | 1826264590246215680 |
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| author | Pike, A Brzozowski, A Hubbard, R |
| author_facet | Pike, A Brzozowski, A Hubbard, R |
| author_sort | Pike, A |
| collection | OXFORD |
| description | Here we review the results that have emerged from our structural studies on the oestrogen receptor ligand-binding domain (ER-LBD). The effects of agonists and antagonists on the structure of ERalpha- and ERbeta-LBDs are examined. In addition, the findings from structural studies of ER-LBD in complex with peptide fragments corresponding to the NR-box II and III modules of the p160 coactivator TIF2 are discussed in the context of the assembly of ER:coactivator complexes. Together these studies have broadened our understanding of ER function by providing a unique insight into ER's ligand specificity, it's ability to interact with coactivators and the structural changes that underlie receptor agonism and antagonism. |
| first_indexed | 2024-03-06T20:10:16Z |
| format | Journal article |
| id | oxford-uuid:2a50e70f-fe5b-4c44-94ce-ff7bdd5f7eb3 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T20:10:16Z |
| publishDate | 2000 |
| record_format | dspace |
| spelling | oxford-uuid:2a50e70f-fe5b-4c44-94ce-ff7bdd5f7eb32022-03-26T12:24:20ZA structural biologist's view of the oestrogen receptor.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:2a50e70f-fe5b-4c44-94ce-ff7bdd5f7eb3EnglishSymplectic Elements at Oxford2000Pike, ABrzozowski, AHubbard, RHere we review the results that have emerged from our structural studies on the oestrogen receptor ligand-binding domain (ER-LBD). The effects of agonists and antagonists on the structure of ERalpha- and ERbeta-LBDs are examined. In addition, the findings from structural studies of ER-LBD in complex with peptide fragments corresponding to the NR-box II and III modules of the p160 coactivator TIF2 are discussed in the context of the assembly of ER:coactivator complexes. Together these studies have broadened our understanding of ER function by providing a unique insight into ER's ligand specificity, it's ability to interact with coactivators and the structural changes that underlie receptor agonism and antagonism. |
| spellingShingle | Pike, A Brzozowski, A Hubbard, R A structural biologist's view of the oestrogen receptor. |
| title | A structural biologist's view of the oestrogen receptor. |
| title_full | A structural biologist's view of the oestrogen receptor. |
| title_fullStr | A structural biologist's view of the oestrogen receptor. |
| title_full_unstemmed | A structural biologist's view of the oestrogen receptor. |
| title_short | A structural biologist's view of the oestrogen receptor. |
| title_sort | structural biologist s view of the oestrogen receptor |
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