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Estrogen receptor transcription and transactivation: Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors
Estrogen receptors are members of the nuclear receptor steroid family that exhibit specific structural features, ligand-binding domain sequence identity and dimeric interactions, that single them out. The crystal structures of their DNA-binding domains give some insight into how nuclear receptors di...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2000
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC138657/ https://www.ncbi.nlm.nih.gov/pubmed/11250728 http://dx.doi.org/10.1186/bcr80 |
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author | Ruff, Marc Gangloff, Monique Marie Wurtz, Jean Moras, Dino |
author_facet | Ruff, Marc Gangloff, Monique Marie Wurtz, Jean Moras, Dino |
author_sort | Ruff, Marc |
collection | PubMed |
description | Estrogen receptors are members of the nuclear receptor steroid family that exhibit specific structural features, ligand-binding domain sequence identity and dimeric interactions, that single them out. The crystal structures of their DNA-binding domains give some insight into how nuclear receptors discriminate between DNA response elements. The various ligand-binding domain crystal structures of the two known estrogen receptor isotypes (α and β) allow one to interpret ligand specificity and reveal the interactions responsible for stabilizing the activation helix H12 in the agonist and antagonist positions. |
format | Text |
id | pubmed-138657 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2000 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-1386572003-02-27 Estrogen receptor transcription and transactivation: Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors Ruff, Marc Gangloff, Monique Marie Wurtz, Jean Moras, Dino Breast Cancer Res Review Estrogen receptors are members of the nuclear receptor steroid family that exhibit specific structural features, ligand-binding domain sequence identity and dimeric interactions, that single them out. The crystal structures of their DNA-binding domains give some insight into how nuclear receptors discriminate between DNA response elements. The various ligand-binding domain crystal structures of the two known estrogen receptor isotypes (α and β) allow one to interpret ligand specificity and reveal the interactions responsible for stabilizing the activation helix H12 in the agonist and antagonist positions. BioMed Central 2000 2000-07-07 /pmc/articles/PMC138657/ /pubmed/11250728 http://dx.doi.org/10.1186/bcr80 Text en Copyright © 2000 Current Science Ltd |
spellingShingle | Review Ruff, Marc Gangloff, Monique Marie Wurtz, Jean Moras, Dino Estrogen receptor transcription and transactivation: Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors |
title | Estrogen receptor transcription and transactivation: Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors |
title_full | Estrogen receptor transcription and transactivation: Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors |
title_fullStr | Estrogen receptor transcription and transactivation: Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors |
title_full_unstemmed | Estrogen receptor transcription and transactivation: Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors |
title_short | Estrogen receptor transcription and transactivation: Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors |
title_sort | estrogen receptor transcription and transactivation: structure-function relationship in dna- and ligand-binding domains of estrogen receptors |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC138657/ https://www.ncbi.nlm.nih.gov/pubmed/11250728 http://dx.doi.org/10.1186/bcr80 |
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