Abstract
The two zinc fingers of the DNA binding domain of the human retinoic acid receptor-beta were labelled with 113Cd. 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 113Cd-1H coupling constant substantially smaller than those of the other metal binding cysteines.
| Original language | English |
|---|---|
| Pages (from-to) | 492-8 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 192 |
| Issue number | 2 |
| Publication status | Published - 30 Apr 1993 |
Keywords
- Amino Acid Sequence
- Binding Sites
- Cadmium
- Carrier Proteins
- Cysteine
- DNA
- Humans
- Isotopes
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Receptors, Retinoic Acid
- Tretinoin
- Zinc