Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA

By B. F. Luisi, W. Xu, Zbyszek Otwinowski, Leonard P. Freedman, Keith R. Yamamoto, P. Sigler. Nature, 2003

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Molecular and cellular endocrinology (2000, neutral): “Gel shifts were visualised with a streptavidin-horseradish peroxidase followed by chemiluminescent detection.”
Overview of Nomenclature of Nuclear Receptors (2006, background): “The crystal structure of the GR and ER DBDs bound to IR3 elements revealed a “head-to-head” protein dimer bound to DNA (Luisi et al., 1991; Schwabe et al., 1993).”
DNA binding and cleavage by the nuclear intron-encoded homing endonuclease I-PpoI (1998, background): “Previous structural studies have visualized three DNA-binding protein families containing two bound zinc ions per protein subunit: steroid receptor”
Origins of specificity in protein-DNA recognition (2010, positive): “For example, in specifically designed noncognate GR complexes, the DNA is able to distort so as to maximize the number of cognate interface interactions, even if these are only maintained by a single strand (102, 112).”
Steroid hormone receptors: an update. (2000, background): “Each HRE half-site is recognized by one receptor monomer (Luisi et al., 1991).”
The glucocorticoid receptor inhibits NFkappaB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain. (2000, methodology): “tion of all known GR target genes (Schena et al. 1989; Luisi et al. 1991).”