The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements
- PMID: 8221895
- DOI: 10.1016/0092-8674(93)90390-c
The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements
Abstract
The nuclear hormone receptors are a superfamily of ligand-activated DNA-binding transcription factors. We have determined the crystal structure (at 2.4 A) of the fully specific complex between the DNA-binding domain from the estrogen receptor and DNA. The protein binds as a symmetrical dimer to its palindromic binding site consisting of two 6 bp consensus half sites with three intervening base pairs. This structure reveals how the protein recognizes its own half site sequence rather than that of the related glucocorticoid receptor, which differs by only two base pairs. Since all nuclear hormone receptors recognize one or the other of these two consensus half site sequences, this recognition mechanism applies generally to the whole receptor family.
Similar articles
-
Binding of the estrogen receptor to DNA. The role of waters.Biophys J. 1997 Aug;73(2):557-70. doi: 10.1016/S0006-3495(97)78093-7. Biophys J. 1997. PMID: 9251777 Free PMC article.
-
The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex.Nat Struct Biol. 1995 May;2(5):386-94. doi: 10.1038/nsb0595-386. Nat Struct Biol. 1995. PMID: 7664096
-
The oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation.Structure. 1995 Feb 15;3(2):201-13. doi: 10.1016/s0969-2126(01)00150-2. Structure. 1995. PMID: 7735836
-
On the mechanism of DNA binding by nuclear hormone receptors: a structural and functional perspective.J Cell Biochem. 1993 Feb;51(2):140-50. doi: 10.1002/jcb.240510205. J Cell Biochem. 1993. PMID: 8440748 Review.
-
DNA-binding by the glucocorticoid receptor: a structural and functional analysis.J Steroid Biochem Mol Biol. 1992 Mar;41(3-8):249-72. doi: 10.1016/0960-0760(92)90351-i. J Steroid Biochem Mol Biol. 1992. PMID: 1562506 Review.
Cited by
-
A role for HDJ-2/HSDJ in correcting subnuclear trafficking, transactivation, and transrepression defects of a glucocorticoid receptor zinc finger mutant.Mol Biol Cell. 1997 May;8(5):795-809. doi: 10.1091/mbc.8.5.795. Mol Biol Cell. 1997. PMID: 9168467 Free PMC article.
-
Asymmetric dimerization in a transcription factor superfamily is promoted by allosteric interactions with DNA.Nucleic Acids Res. 2023 Sep 8;51(16):8864-8879. doi: 10.1093/nar/gkad632. Nucleic Acids Res. 2023. PMID: 37503845 Free PMC article.
-
Binding of the estrogen receptor to DNA. The role of waters.Biophys J. 1997 Aug;73(2):557-70. doi: 10.1016/S0006-3495(97)78093-7. Biophys J. 1997. PMID: 9251777 Free PMC article.
-
The dimerization interfaces formed between the DNA binding domains of RXR, RAR and TR determine the binding specificity and polarity of the full-length receptors to direct repeats.EMBO J. 1994 Mar 15;13(6):1425-33. doi: 10.1002/j.1460-2075.1994.tb06396.x. EMBO J. 1994. PMID: 8137826 Free PMC article.
-
Determinants of target gene specificity for ROR alpha 1: monomeric DNA binding by an orphan nuclear receptor.Mol Cell Biol. 1995 May;15(5):2517-26. doi: 10.1128/MCB.15.5.2517. Mol Cell Biol. 1995. PMID: 7739535 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases