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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...

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Detalles Bibliográficos
Autores principales: Ruff, Marc, Gangloff, Monique, Marie Wurtz, Jean, Moras, Dino
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2000
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.
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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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