Nuclear receptor antagonists designed based on the helix-folding inhibition hypothesis.
Here we review our studies on the molecular design of nuclear receptor antagonists, including retinoic acid receptor (RAR) antagonists, retinoid X receptor (RXR) antagonists, androgen receptor (AR) antagonists, and vitamin D receptor (VDR) antagonists, based on inhibition of folding of helix 12, which contains a co-activator binding site. Recent progress in structural development studies of peroxisome proliferator-activated receptor (PPAR) ligands is also reviewed.
Hashimoto
Yuichi
Y
Institute of Molecular & Cellular Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan. bmcyfh@iam.u-tokyo.ac.jp
Miyachi
Hiroyuki
H
D008024:Ligands; D015394:Molecular Structure; D018160:Receptors, Cytoplasmic and Nuclear / Q000037:antagonists & inhibitors*
D008024:Ligands; D018160:Receptors, Cytoplasmic and Nuclear