Crystallization of the human glucocorticoid receptor ligand binding domain: a step towards selective glucocorticoids.
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.
Necela
Brian M
BM
Laboratory of Signal Transduction, Building 101, MD F3-07, Department of Health and Human Services, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA.
Cidlowski
John A
JA
D000818:Animals; D001665:Binding Sites / Q000502:physiology; D003460:Crystallization; D006801:Humans; D008024:Ligands; D011965:Receptors, Glucocorticoid / Q000737:chemistry* / Q000378:metabolism*
D008024:Ligands; D011965:Receptors, Glucocorticoid