The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: How receptors discriminate between their response elements

  title={The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: How receptors discriminate between their response elements},
  author={John W. R. Schwabe and Lynda Chapman and John T. Finch and Daniela Rhodes},
Importance of the Sequence-Directed DNA Shape for Specific Binding Site Recognition by the Estrogen-Related Receptor
The results suggest that the sequence-directed DNA shape is more important than the exact nucleotide sequence for the binding of ERR DBD to DNA as a dimer, and underlines the importance of the shape-driven DNA readout mechanisms based on minor groove recognition and electrostatic potential.
Structural basis for nuclear hormone receptor DNA binding
Estrogen receptor transcription and transactivation: Structure-function relationship in DNA- and ligand-binding domains of estrogen receptors
The various ligand-binding domain crystal structures of the two known estrogen receptor isotypes allow one to interpret ligand specificity and reveal the interactions responsible for stabilizing the activation helix H12 in the agonist and antagonist positions.
Structural basis of RXR-DNA interactions.
The structure shows how a gene-regulatory site can induce conformational changes in a transcription factor that promote homo-cooperative assembly and illustrates how site selection is achieved in this large eukaryotic transcription factor family through discrete protein-protein interactions and the use of tandem DNA binding sites with characteristic spacings.
Structural determinants of nuclear receptor assembly on DNA direct repeats
The stereochemistry suggests a mechanism by which heterodimers recognize the inter-half-site spacing between direct repeats of the consensus sequence 5′-AGGTCA-3′ separated by one to five base pairs.
Analysis of the DNA-binding affinity, sequence specificity and context dependence of the glucocorticoid receptor zinc finger region.
Findings indicate that the consensus core motif alone is not sufficient to specify a functional RBS, and that flanking sequences create an appropriate context for protein binding, as certain mutations at these positions reduced binding drastically.
NMR Spectroscopic Studies of the DNA-binding Domain of the Monomer-binding Nuclear Orphan Receptor, Human Estrogen Related Receptor-2
The CTE element of hERR2 is unstructured and highly flexible, exhibiting nearly random coil chemical shifts, extreme sensitivity of the backbone amide protons to solvent presaturation, and reduced heteronuclear {1H-15N} nuclear Overhauser effect values.


Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA
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
Solution structure of the glucocorticoid receptor DNA-binding domain.
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.
The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain
It is reported here that a protein of relative molecular mass 19,000 encompassing the DNA-binding domain of the glucocorticoid receptor that has been overexpressed in Escherichia coli and purified to homogeneity reversibly ligates two Zn(II) or Cd( II) ions.
Defining a minimal estrogen receptor DNA binding domain.
The results indicate that in addition to the zinc finger core, amino acids C-terminal to the core in regions C and D play a key role in DNA binding by the ER, particularly to imperfectly palindromic response elements.
Solution structure of the DMA-binding domain of the oestrogen receptor
The structure of the DNA-binding domain from the oestrogen receptor, as determined by two-dimensional 1H NMR techniques, seems to be a general structure for protein-DNA recognition.
Cooperativity and specificity in the interactions between DNA and the glucocorticoid receptor DNA-binding domain.
It is found that binding to both DNAs is cooperative but that DBDr shows a higher affinity for the GRE than for nonspecific DNA and that this difference is more pronounced at increased salt concentrations.
Structure of the retinoid X receptor alpha DNA binding domain: a helix required for homodimeric DNA binding.
The three-dimensional solution structure of the DNA binding domain (DBD) of the retinoid X receptor alpha (RXR alpha) was determined by nuclear magnetic resonance spectroscopy to define a structural feature required for selective dimerization of the RXR on hormone response elements composed of half-sites (5'-AGGTCA-3') arranged as tandem repeats.
Differential orientations of the DNA-binding domain and carboxy-terminal dimerization interface regulate binding site selection by nuclear receptor heterodimers.
Evidence is presented that the preference for direct repeat elements arises from two fundamental differences from steroid hormone receptors, and several independent lines of evidence suggest that the DNA-binding domain of the thyroid hormone receptor is preferentially rotated by approximately 180 degrees with respect to its carboxy-terminal dimerization interface.
1H NMR studies of DNA recognition by the glucocorticoid receptor: complex of the DNA binding domain with a half-site response element.
The complex of the rat glucocorticoid receptor (GR) DNA binding domain (DBD) and half-site sequence of the consensus glucoc Corticoid response element (GRE) has been studied by two-dimensional 1H NMR spectroscopy and findings are consistent with the model proposed by Härd et al.