Crystallization of the human glucocorticoid receptor ligand binding domain: a step towards selective glucocorticoids

• Autores: Brian M. Necela, John A. Cidlowski
• Localización: Trends in pharmacological sciences, ISSN 0165-6147, Vol. 24, Nº. 2 (February), 2003, págs. 58-60
• Idioma: inglés
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• Resumen

  • The crystal structure of the glucocorticoid receptor (GR) ligand binding domain in a ternary complex with dexamethasone and a TIF2 coactivator peptide has been determined recently. The structure reveals several distinct features not found in other nuclear receptors, such as a novel dimerization interface and a second charge clamp that might be important in determining coactivator binding selectivity. The GR ligand binding domain also has a steroid binding pocket that is distinct from other nuclear receptors and might explain its selectivity for glucocorticoids and its diversity of responses