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The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements.
- Source :
-
Cell [Cell] 1993 Nov 05; Vol. 75 (3), pp. 567-78. - Publication Year :
- 1993
-
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.
- Subjects :
- Amino Acid Sequence
Base Composition
Base Sequence
Binding Sites
Consensus Sequence
Crystallography, X-Ray
Gene Expression Regulation
Hydrogen Bonding
Macromolecular Substances
Models, Molecular
Molecular Sequence Data
Protein Conformation
Receptors, Glucocorticoid chemistry
DNA chemistry
Receptors, Estrogen chemistry
Regulatory Sequences, Nucleic Acid
Subjects
Details
- Language :
- English
- ISSN :
- 0092-8674
- Volume :
- 75
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Cell
- Publication Type :
- Academic Journal
- Accession number :
- 8221895
- Full Text :
- https://doi.org/10.1016/0092-8674(93)90390-c