1R4O

Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA

1R4O の概要

• エントリーDOI: 10.2210/pdb1r4o/pdb
• 関連するPDBエントリー: 1GLU 1R4R
• 分子名称: 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)
• 機能のキーワード: gr, steroid receptor, protein-dna complex, glucocorticoid, transcription-dna complex, transcription/dna
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Cytoplasm (By similarity): P06536
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 32335.51

構造登録者

Luisi, B.F.,Xu, W.X.,Otwinowski, Z.,Freedman, L.P.,Yamamoto, K.R.,Sigler, P.B. (登録日: 2003-10-07, 公開日: 2003-10-21, 最終更新日: 2023-08-23)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)