Issue 31, 2020

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

Abstract

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.

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

Supplementary files

Article information

Article type
Communication
Submitted
15 Jun 2020
Accepted
20 Jul 2020
First published
29 Jul 2020

Org. Biomol. Chem., 2020,18, 6063-6071

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

R. Pokhrel, T. Tang and J. M. Holub, Org. Biomol. Chem., 2020, 18, 6063 DOI: 10.1039/D0OB01234C

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