Kim, HY Pae, AN Lee, YJ Park, J Kim, DS Hwang, KY Yu, MH Kim, EE 2024-01-21T05:41:05Z 2024-01-21T05:41:05Z 2021-09-05 2005-01 1013-9826 https://pubs.kist.re.kr/handle/201004/136876 Estrogen-related receptors (ERRs), orphan nuclear receptors, share a significant amino acid sequence homology with estrogen receptors (ERs), yet their ligands do not respond in the same manner. In fact, some of the ligands that are known as agonists of ERs show antagonistic effect in ERRs. Accordingly, the current study investigated the structures of the ligand-binding domains using homology model building and docking studies. The results showed clear differences between the ligand-binding pockets of ERRs and ERs, thereby providing structural insights into the activities related to the ligands. English TRANS TECH PUBLICATIONS LTD INDEPENDENT TRANSCRIPTIONAL ACTIVATION ERR COACTIVATOR ALPHA-1 GAMMA BETA Structural comparison of ligand-binding domains in estrogen-related receptors Article 10.4028/www.scientific.net/KEM.277-279.107 1 ON THE CONVERGENCE OF BIO-INFORMATION-, ENVIRONMENTAL-, ENERGY-, SPACE- AND NANO-TECHNOLOGIES, PTS 1 AND 2, v.277-279, pp.107 - 112 ON THE CONVERGENCE OF BIO-INFORMATION-, ENVIRONMENTAL-, ENERGY-, SPACE- AND NANO-TECHNOLOGIES, PTS 1 AND 2 277-279 107 112 scie scopus 000227164500020 2-s2.0-33646067701 Engineering, Multidisciplinary Materials Science, Ceramics Materials Science, Composites Engineering Materials Science Article; Proceedings Paper INDEPENDENT TRANSCRIPTIONAL ACTIVATION ERR COACTIVATOR ALPHA-1 GAMMA BETA orphan nuclear receptor estrogen related receptor (ERR) estrogen receptor (ER) ligand-binding domain diethylstilbestrol (DES) 4-hydroxyltamoxifen (OHT) homology modeling