Heteronuclear 113Cd-1H NMR study of metal coordination in the human retinoic acid receptor-beta DNA binding domain.
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.
Knegtel
R M
RM
Department of Chemistry, University of Utrecht, The Netherlands.
Boelens
R
R
Ganadu
M L
ML
George
A V
AV
van der Saag
P T
PT
Kaptein
R
R
D000595:Amino Acid Sequence; D001665:Binding Sites; D002104:Cadmium; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D003545:Cysteine / Q000737:chemistry; D004247:DNA / Q000378:metabolism*; D006801:Humans; D007554:Isotopes; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D018168:Receptors, Retinoic Acid; D014212:Tretinoin / Q000378:metabolism*; D015032:Zinc / Q000737:chemistry*
D002352:Carrier Proteins; D007554:Isotopes; D018168:Receptors, Retinoic Acid; D002104:Cadmium; D014212:Tretinoin; D004247:DNA; D015032:Zinc; D003545:Cysteine