Monitoring ligand-mediated helix 12 transitions within the human estrogen receptor α using bipartite tetracysteine display

Org Biomol Chem. 2020 Aug 21;18(31):6063-6071. doi: 10.1039/d0ob01234c. Epub 2020 Jul 29.


Estrogen receptor α ligand-binding domains (ERα-LBD) expressing tetracysteine motifs bind FlAsH-EDT2 upon transition of helix 12 (H12) to a folded state. Changes in fluorescence intensity allowed surveillance of ligand-mediated H12 transitions and facilitated the determination of FlAsH association rates (kon) and apparent equilibrium dissociation constants (Kapp) to ERα-LBDs in the presence of estrogenic ligands.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cysteine / analogs & derivatives
  • Cysteine / chemistry
  • Cysteine / metabolism*
  • Estrogen Receptor alpha / chemistry
  • Estrogen Receptor alpha / genetics
  • Estrogen Receptor alpha / metabolism*
  • Humans
  • Ligands
  • Models, Molecular
  • Mutation


  • ESR1 protein, human
  • Estrogen Receptor alpha
  • Ligands
  • Cysteine