Heteronuclear 113Cd-1H NMR study of metal coordination in the human retinoic acid receptor-β DNA binding domain

R.M.A. Knegtel, R. Boelens, M.L. Ganadu, A.V.E. George, P.T. Van der Saag, R. Kaptein

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

The two zinc fingers of the DNA binding domain of the human retinoic acid receptor-β 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 languageEnglish
Pages (from-to)492-498
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume192
Issue number2
DOIs
Publication statusPublished - 29 Jan 1993

Keywords

  • cadmium
  • retinoic acid binding protein
  • zinc finger protein
  • article
  • binding site
  • priority journal
  • protein DNA binding
  • proton nuclear magnetic resonance

Fingerprint

Dive into the research topics of 'Heteronuclear 113Cd-1H NMR study of metal coordination in the human retinoic acid receptor-β DNA binding domain'. Together they form a unique fingerprint.

Cite this