Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA

B. F. Luisi, W. X. Xu, Z. Otwinowski, L. P. Freedman, K. R. Yamamoto, P. B. Sigler

Research output: Contribution to journalArticlepeer-review

1228 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)497-505
Number of pages9
Issue number6335
StatePublished - Jan 1 1991

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA'. Together they form a unique fingerprint.

Cite this