1R4O

Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA

Summary for 1R4O

• Entry DOI: 10.2210/pdb1r4o/pdb
• Related: 1GLU 1R4R
• Descriptor: 5'-D(*CP*CP*AP*GP*AP*AP*CP*AP*TP*CP*GP*AP*TP*GP*TP*TP*CP*TP*G)-3', Glucocorticoid receptor, ZINC ION, ... (4 entities in total)
• Functional Keywords: gr, steroid receptor, protein-dna complex, glucocorticoid, transcription-dna complex, transcription/dna
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cytoplasm (By similarity): P06536
• Total number of polymer chains: 4
• Total formula weight: 32335.51

Authors

Luisi, B.F.,Xu, W.X.,Otwinowski, Z.,Freedman, L.P.,Yamamoto, K.R.,Sigler, P.B. (deposition date: 2003-10-07, release date: 2003-10-21, Last modification date: 2023-08-23)

Primary citation

Luisi, B.F.,Xu, W.X.,Otwinowski, Z.,Freedman, L.P.,Yamamoto, K.R.,Sigler, P.B.
Crystallographic Analysis of the Interaction of The Glucocorticoid Receptor with DNA
Nature, 352:497-505, 1991

PubMed Abstract: Two crystal structures of the glucocorticoid receptor DNA-binding domain complexed with DNA are reported. The domain has a globular fold which contains two Zn-nucleated substructures of distinct conformation and function. When it binds DNA, the domain dimerizes, placing the subunits in adjacent major grooves. In one complex, the DNA has the symmetrical consensus target sequence; in the second, the central spacing between the target's half-sites is larger by one base pair. This results in one subunit interacting specifically with the consensus target half-site and the other nonspecifically with a noncognate element. The DNA-induced dimer fixes the separation of the subunits' recognition surfaces so that the spacing between the half-sites becomes a critical feature of the target sequence's identity.

PubMed: 1865905
DOI: 10.1038/352497a0

Experimental method

X-RAY DIFFRACTION (2.5 Å)