3G9O

GR DNA-binding domain:Sgk 16bp complex-9

Summary for 3G9O

• Entry DOI: 10.2210/pdb3g9o/pdb
• Related: 3FYL 3G6P 3G6Q 3G6R 3G6T 3G6U 3G8U 3G8X 3G97 3G99 3G9I 3G9J 3G9M 3G9P
• Descriptor: Glucocorticoid receptor, DNA (5'-D(*TP*CP*GP*GP*AP*CP*AP*AP*AP*AP*TP*GP*TP*TP*CP*T)-3'), DNA (5'-D(*AP*AP*GP*AP*AP*CP*AP*TP*TP*TP*TP*GP*TP*CP*CP*G)-3'), ... (5 entities in total)
• Functional Keywords: glucocorticoid, dna-binding, allostery, lever arm, transcription, hormone, alternative initiation, chromatin regulator, cytoplasm, lipid-binding, metal-binding, nucleus, phosphoprotein, polymorphism, receptor, steroid-binding, transcription regulation, ubl conjugation, zinc, zinc-finger, transcription-dna complex, transcription/dna
• Biological source: Rattus norvegicus (brown rat,rat,rats)
• Cellular location: Cytoplasm (By similarity): P06536
• Total number of polymer chains: 4
• Total formula weight: 29981.56

Authors

Pufall, M.A.,Yamamoto, K.R.,Meijsing, S.H. (deposition date: 2009-02-13, release date: 2009-04-21, Last modification date: 2023-09-06)

Primary citation

Meijsing, S.H.,Pufall, M.A.,So, A.Y.,Bates, D.L.,Chen, L.,Yamamoto, K.R.
DNA binding site sequence directs glucocorticoid receptor structure and activity.
Science, 324:407-410, 2009

PubMed Abstract: Genes are not simply turned on or off, but instead their expression is fine-tuned to meet the needs of a cell. How genes are modulated so precisely is not well understood. The glucocorticoid receptor (GR) regulates target genes by associating with specific DNA binding sites, the sequences of which differ between genes. Traditionally, these binding sites have been viewed only as docking sites. Using structural, biochemical, and cell-based assays, we show that GR binding sequences, differing by as little as a single base pair, differentially affect GR conformation and regulatory activity. We therefore propose that DNA is a sequence-specific allosteric ligand of GR that tailors the activity of the receptor toward specific target genes.

PubMed: 19372434
DOI: 10.1126/science.1164265

Experimental method

X-RAY DIFFRACTION (1.65 Å)