BIOMAT Database Logo BIOMAT Database Logo

Solution structure of the glucocorticoid receptor DNA-binding domain. 1990

T Härd, and E Kellenbach, and R Boelens, and B A Maler, and K Dahlman, and L P Freedman, and J Carlstedt-Duke, and K R Yamamoto, and J A Gustafsson, and R Kaptein
Department of Chemistry, University of Utrecht, The Netherlands.

The three-dimensional structure of the DNA-binding domain (DBD) of the glucocorticoid receptor has been determined by nuclear magnetic resonance spectroscopy and distance geometry. The structure of a 71-residue protein fragment containing two "zinc finger" domains is based on a large set of proton-proton distances derived from nuclear Overhauser enhancement spectra, hydrogen bonds in previously identified secondary structure elements, and coordination of two zinc atoms by conserved cysteine residues. The DBD is found to consist of a globular body from which the finger regions extend. A model of the dimeric complex between the DBD and the glucocorticoid response element is proposed. The model is consistent with previous results indicating that specific amino acid residues of the DBD are involved in protein-DNA and protein-protein interactions.

UI MeSH Term Description Entries
D008667 Metalloproteins Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed) Metalloprotein
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009682 Magnetic Resonance Spectroscopy Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING). In Vivo NMR Spectroscopy,MR Spectroscopy,Magnetic Resonance,NMR Spectroscopy,NMR Spectroscopy, In Vivo,Nuclear Magnetic Resonance,Spectroscopy, Magnetic Resonance,Spectroscopy, NMR,Spectroscopy, Nuclear Magnetic Resonance,Magnetic Resonance Spectroscopies,Magnetic Resonance, Nuclear,NMR Spectroscopies,Resonance Spectroscopy, Magnetic,Resonance, Magnetic,Resonance, Nuclear Magnetic,Spectroscopies, NMR,Spectroscopy, MR
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011965 Receptors, Glucocorticoid Cytoplasmic proteins that specifically bind glucocorticoids and mediate their cellular effects. The glucocorticoid receptor-glucocorticoid complex acts in the nucleus to induce transcription of DNA. Glucocorticoids were named for their actions on blood glucose concentration, but they have equally important effects on protein and fat metabolism. Cortisol is the most important example. Corticoid Type II Receptor,Glucocorticoid Receptors,Glucocorticoids Receptor,Corticoid II Receptor,Corticoid Type II Receptors,Glucocorticoid Receptor,Receptors, Corticoid II,Receptors, Corticoid Type II,Receptors, Glucocorticoids,Corticoid II Receptors,Glucocorticoids Receptors,Receptor, Corticoid II,Receptor, Glucocorticoid,Receptor, Glucocorticoids
D012045 Regulatory Sequences, Nucleic Acid Nucleic acid sequences involved in regulating the expression of genes. Nucleic Acid Regulatory Sequences,Regulatory Regions, Nucleic Acid (Genetics),Region, Regulatory,Regions, Regulatory,Regulator Regions, Nucleic Acid,Regulatory Region,Regulatory Regions
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D004268 DNA-Binding Proteins Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases. DNA Helix Destabilizing Proteins,DNA-Binding Protein,Single-Stranded DNA Binding Proteins,DNA Binding Protein,DNA Single-Stranded Binding Protein,SS DNA BP,Single-Stranded DNA-Binding Protein,Binding Protein, DNA,DNA Binding Proteins,DNA Single Stranded Binding Protein,DNA-Binding Protein, Single-Stranded,Protein, DNA-Binding,Single Stranded DNA Binding Protein,Single Stranded DNA Binding Proteins

Related Publications

T Härd, and E Kellenbach, and R Boelens, and B A Maler, and K Dahlman, and L P Freedman, and J Carlstedt-Duke, and K R Yamamoto, and J A Gustafsson, and R Kaptein
Refined solution structure of the glucocorticoid receptor DNA-binding domain.
December 1993, Biochemistry,
T Härd, and E Kellenbach, and R Boelens, and B A Maler, and K Dahlman, and L P Freedman, and J Carlstedt-Duke, and K R Yamamoto, and J A Gustafsson, and R Kaptein
Solution structure of the DNA-binding domain of the oestrogen receptor.
November 1990, Nature,
T Härd, and E Kellenbach, and R Boelens, and B A Maler, and K Dahlman, and L P Freedman, and J Carlstedt-Duke, and K R Yamamoto, and J A Gustafsson, and R Kaptein
High-resolution solution structure of the retinoid X receptor DNA-binding domain.
August 1998, Journal of molecular biology,
T Härd, and E Kellenbach, and R Boelens, and B A Maler, and K Dahlman, and L P Freedman, and J Carlstedt-Duke, and K R Yamamoto, and J A Gustafsson, and R Kaptein
Backbone dynamics of the glucocorticoid receptor DNA-binding domain.
December 1992, Biochemistry,
T Härd, and E Kellenbach, and R Boelens, and B A Maler, and K Dahlman, and L P Freedman, and J Carlstedt-Duke, and K R Yamamoto, and J A Gustafsson, and R Kaptein
The solution structure of the human retinoic acid receptor-beta DNA-binding domain.
January 1993, Journal of biomolecular NMR,
T Härd, and E Kellenbach, and R Boelens, and B A Maler, and K Dahlman, and L P Freedman, and J Carlstedt-Duke, and K R Yamamoto, and J A Gustafsson, and R Kaptein
Solution structure of the DNA-binding domain of MafG.
April 2002, Nature structural biology,
T Härd, and E Kellenbach, and R Boelens, and B A Maler, and K Dahlman, and L P Freedman, and J Carlstedt-Duke, and K R Yamamoto, and J A Gustafsson, and R Kaptein
Solution structure of the DNA-binding domain of TraM.
March 2001, Biochemistry,
T Härd, and E Kellenbach, and R Boelens, and B A Maler, and K Dahlman, and L P Freedman, and J Carlstedt-Duke, and K R Yamamoto, and J A Gustafsson, and R Kaptein
Structure and function of the glucocorticoid receptor ligand binding domain.
January 2004, Vitamins and hormones,
T Härd, and E Kellenbach, and R Boelens, and B A Maler, and K Dahlman, and L P Freedman, and J Carlstedt-Duke, and K R Yamamoto, and J A Gustafsson, and R Kaptein
Protein-protein interactions facilitate DNA binding by the glucocorticoid receptor DNA-binding domain.
August 1990, The Journal of biological chemistry,
T Härd, and E Kellenbach, and R Boelens, and B A Maler, and K Dahlman, and L P Freedman, and J Carlstedt-Duke, and K R Yamamoto, and J A Gustafsson, and R Kaptein
Molecular dynamics simulations of the glucocorticoid receptor DNA-binding domain in complex with DNA and free in solution.
February 1995, Biophysical journal,
Copied contents to your clipboard!