More than meets the dimer: What is the quaternary structure of the glucocorticoid receptor?
It is widely accepted that the glucocorticoid receptor (GR), a ligand-regulated transcription factor that triggers anti-inflammatory responses, binds specific response elements as a homodimer. Here, we will discuss the original primary data that established this model and contrast it with a recent r...
| Autores: | , |
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| Tipo de documento: | artigo |
| Estado: | Versão publicada |
| Data de publicação: | 2017 |
| País: | Argentina |
| Recursos: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositório: | CONICET Digital (CONICET) |
| Idioma: | inglês |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/64876 |
| Acesso em linha: | http://hdl.handle.net/11336/64876 |
| Access Level: | Acceso aberto |
| Palavra-chave: | DIMER DNA BINDING GLUCOCORTICOID RECEPTOR MONOMER STEROID RECEPTORS TETRAMER https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| Resumo: | It is widely accepted that the glucocorticoid receptor (GR), a ligand-regulated transcription factor that triggers anti-inflammatory responses, binds specific response elements as a homodimer. Here, we will discuss the original primary data that established this model and contrast it with a recent report characterizing the GR–DNA complex as a tetramer. |
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