Necela Brian M, Cidlowski John A
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.
Trends Pharmacol Sci. 2003 Feb;24(2):58-61. doi: 10.1016/S0165-6147(02)00046-9.
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.
最近已确定了糖皮质激素受体（GR）配体结合域与地塞米松和一种TIF2共激活剂肽形成的三元复合物的晶体结构。该结构揭示了其他核受体中未发现的几个独特特征，例如一个新的二聚化界面和第二个电荷钳，这可能在确定共激活剂结合选择性方面很重要。GR配体结合域还有一个与其他核受体不同的类固醇结合口袋，这可能解释了其对糖皮质激素的选择性及其反应的多样性。
