Expression, purification, and characterization of multiple, multifunctional human glucocorticoid receptor proteins.
Détails
ID Serval
serval:BIB_AD700B476BC5
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Expression, purification, and characterization of multiple, multifunctional human glucocorticoid receptor proteins.
Périodique
Protein expression and purification
ISSN
1096-0279 (Electronic)
ISSN-L
1046-5928
Statut éditorial
Publié
Date de publication
11/2008
Peer-reviewed
Oui
Volume
62
Numéro
1
Pages
29-35
Langue
anglais
Notes
Publication types: Journal Article
Publication Status: ppublish
Publication Status: ppublish
Résumé
The glucocorticoid receptor (GR) is a nuclear receptor protein that plays a central role in glucose homeostasis, the stress response, control of the hypothalamic-pituitary-adrenal axis, and immuno-inflammatory processes via binding of the natural steroid, cortisol. GR is a well-validated drug target and continues to be an important target for new drug discovery efforts. Here, we describe a basic and simple method for Escherichia coli expression and purification of a variety of human GR proteins that contain all three of the functional domains of the protein: the activation function-1 domain, the DNA-binding domain, and the ligand-binding domain. We present characterization data to show that these purified, multifunctional GR proteins are active for ligand, coactivator, and DNA-binding. The work presented here should serve as a reference for future mechanistic, structural and drug discovery efforts that require purified, full or near full length, GR protein.
Mots-clé
Escherichia coli/genetics, Escherichia coli/metabolism, Gene Expression, Humans, Ligands, Receptors, Glucocorticoid/chemistry, Receptors, Glucocorticoid/genetics, Receptors, Glucocorticoid/isolation & purification
Pubmed
Web of science
Création de la notice
29/01/2021 16:30
Dernière modification de la notice
30/01/2021 7:26