Solution structure of the glucocorticoid receptor DNA-binding domain.
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Summary
A model of the dimeric complex between the DBD and the glucocorticoid response element is proposed, consistent with previous results indicating that specific amino acid residues of the D BD are involved in protein-DNA and protein-protein interactions.
- Type
- article
- Published
- 1990-07-13
- Cited by
- 539
- References
- 19
- OpenAlex
- https://openalex.org/W2012324003
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:7089077
Keywords
Zinc finger, Chemistry, DNA-binding domain, Glucocorticoid receptor, Hydrogen bond
References
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- A retroviral Cys-Xaa2-Cys-Xaa4-His-Xaa4-Cys peptide binds metal ions: spectroscopic studies and a proposed three-dimensional structure.
- Three-dimensional solution structure of a single zinc finger DNA-binding domain.
- The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain
- Two amino acids within the knuckle of the first zinc finger specify DNA response element activation by the glucocorticoid receptor.
- Investigation of exchange processes by two‐dimensional NMR spectroscopy
- The steroid and thyroid hormone receptor superfamily.
- Steroid receptor regulated transcription of specific genes and gene networks.
- DNA binding specificity of steroid receptors.
- Biochemistry, molecular biology, and physiology of the glucocorticoid receptor.
Cited by
- Mutations in the "zinc fingers" or in the N-terminal region of the DNA binding domain of the human glucocorticosteroid receptor facilitate its salt-induced transformation, but do not modify hormone binding.
- A 55-kilodalton accessory factor facilitates vitamin D receptor DNA binding.
- Introduction to metallothionein.
- Solution structure of the DNA-binding domain of the oestrogen receptor.
- The Molecular Biology of Thyroid Hormone Action
- DNA binding activity of the glucocorticoid receptor is sensitive to redox changes in intact cells.
- Molecular modeling and in vitro investigations of the human androgen receptor DNA-binding domain: application for the study of two mutations.
- The mosquito ultraspiracle homologue, a partner of ecdysteroid receptor heterodimer: cloning and characterization of isoforms expressed during vitellogenesis.
- Role of hypoxia and hypoxia inducible factors (HIFs) in cells of Ewing’s Sarcoma Family Tumors
- Discovery of novel nuclear receptor modulating ligands: an integral role for peptide interaction profiling.
- The glucocorticoid receptor dimer interface allosterically transmits sequence-specific DNA signals
- Recent advances in the molecular biology of vitamin D action.
- Molecular and genetic characterization of SPT4, a gene important for transcription initiation in Saccharomyces cerevisiae
- Expression, nuclear transport, and phosphorylation of adenovirus DNA replication proteins.
- Salvage enzymes in nucleotide biosynthesis
- Point mutation in the DNA binding domain of the androgen receptor in two families with Reifenstein syndrome.
- Coregulatory proteins in nuclear hormone receptor action.
- Zinc finger‐mediated protein interactions modulate Ikaros activity, a molecular control of lymphocyte development.
- THAP1, un régulateur clé de la prolifération des cellules endothéliales : relations structure/fonction et gènes ciblés
- Thermodynamics of Zn2+ binding to Cys2His2 and Cys2HisCys zinc fingers and a Cys4 transcription factor site.
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