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Structure of the ligand-binding domain of oestrogen receptor beta in the presence of a partial agonist and a full antagonist.

Abstract:

Oestrogens exert their physiological effects through two receptor subtypes. Here we report the three-dimensional structure of the oestrogen receptor beta isoform (ERbeta) ligand-binding domain (LBD) in the presence of the phyto-oestrogen genistein and the antagonist raloxifene. The overall structure of ERbeta-LBD is very similar to that previously reported for ERalpha. Each ligand interacts with a unique set of residues within the hormone-binding cavity and induces a distinct orientation in t...

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Publication status:
Published

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Publisher copy:
10.1093/emboj/18.17.4608

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Journal:
The EMBO journal
Volume:
18
Issue:
17
Pages:
4608-4618
Publication date:
1999-09-05
DOI:
EISSN:
1460-2075
ISSN:
0261-4189
URN:
uuid:a376ec3e-8220-4bc1-adbf-e08bf76a1eda
Source identifiers:
317556
Local pid:
pubs:317556

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