Heteronuclear 113Cd-1H NMR Study of Metal Coordination in the Human Retinoic Acid Receptor-β DNA Binding Domain
| Autor: | Robert Kaptein, Maria Luisa Ganadu, R. M. A. Knegtel, A. V. E. George, Rolf Boelens, P.T. Vandersaag |
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| Rok vydání: | 1993 |
| Předmět: |
Magnetic Resonance Spectroscopy
Receptors Retinoic Acid Stereochemistry Molecular Sequence Data Biophysics Retinoic acid Tretinoin Biochemistry DNA-binding protein chemistry.chemical_compound Isotopes Humans Amino Acid Sequence Cysteine Molecular Biology Zinc finger Binding Sites DNA Cell Biology DNA-binding domain Zinc Retinoic acid receptor Heteronuclear molecule chemistry Proton NMR Carrier Proteins Cadmium |
| Zdroj: | Biochemical and Biophysical Research Communications. 192:492-498 |
| ISSN: | 0006-291X |
| Popis: | The two zinc fingers of the DNA binding domain of the human retinoic acid receptor-β were labelled with 113 Cd. Two- and three-dimensional heteronuclear nuclear magnetic resonance (NMR) experiments show that the first eight conserved cysteine residues coordinate the two zinc ions tetrahedrally. The ninth conserved cysteine is not involved in metal coordination. In each finger one cysteine exhibits a heteronuclear 113 Cd- 1 H coupling constant substantially smaller than those of the other metal binding cysteines. |
| Databáze: | OpenAIRE |
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