Structural basis for agonism and antagonism for a set of chemically related progesterone receptor modulators.
J Biol Chem
; 286(40): 35079-86, 2011 Oct 07.
Article
em En
| MEDLINE
| ID: mdl-21849509
ABSTRACT
The progesterone receptor is able to bind to a large number and variety of ligands that elicit a broad range of transcriptional responses ranging from full agonism to full antagonism and numerous mixed profiles inbetween. We describe here two new progesterone receptor ligand binding domain x-ray structures bound to compounds from a structurally related but functionally divergent series, which show different binding modes corresponding to their agonistic or antagonistic nature. In addition, we present a third progesterone receptor ligand binding domain dimer bound to an agonist in monomer A and an antagonist in monomer B, which display binding modes in agreement with the earlier observation that agonists and antagonists from this series adopt different binding modes.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Receptores de Progesterona
Limite:
Animals
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article