Younchang Kim

TL;DR: The structure of an apo steroid receptor is presented that reveals a ligand-accessible channel allowing soaking of preformed crystals and the structural basis of NFkappaB-selective signaling through the estrogen receptor is defined, thus revealing a unique conformation of the receptor that allows selective suppression of inflammatory gene expression.

TL;DR: The X‐ray crystal structure of the oestrogen receptor α (ERα) bound to an oestradiol derivative with a prosthetic group, ortho‐ trifluoromethlyphenylvinyl, which binds in a novel extended pocket in the ligand‐binding domain is reported.

TL;DR: These studies define the structural determinants of stability and cellular bioactivity of a B-N for C=C substitution in nonsteroidal estrogens and provide a framework for further exploration of "elemental isomerism" for diversification of drug-like molecules.

TL;DR: 2,3-Diarylpyrazolo[1,5-a]pyrimidines analogs that contain a basic side chain at the 2- or 3-aryl group are prepared and shows an increase in binding affinity and antagonist potency and a loss of residual agonist activity.

TL;DR: Corrigendum: NFκB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses suggests thatNFκB ligand selectivity may be related to ‘cell reprograming’ rather than ‘drug-like’ properties.