Structural Comparison of Ligand-Binding Domains in Estrogen-Related Receptors |
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| Journal | Key Engineering Materials (Volumes 277 - 279) |
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| Volume | On the Convergence of Bio-, Information-, Enrivonmental-, Energy-, Space- and Nano-Technolgies |
| Edited by | Kwang Hwa Chung, Yong Hyeon Shin, Sue-Nie Park, Hyun Sook Cho, Soon-Ae Yoo, Byung Joo Min, Hyo-Suk Lim and Kyung Hwa Yoo |
| Pages | 107-112 |
| DOI | 10.4028/www.scientific.net/KEM.277-279.107 |
| Citation | Hye Yeon Kim et al., 2005, Key Engineering Materials, 277-279, 107 |
| Online since | January, 2005 |
| Authors | Hye Yeon Kim, Ae Nim Pae, Yeon Joo Lee, Joon Kyu Park, Dae Sung Kim, Kwang Yeon Hwang, Myeong-Hee Yu, Eunice EunKyeong Kim |
| Keywords | 4-Hydroxyltamoxifen (OHT), Diethylstilbestrol (DES), Estrogen Receptor ER, Estrogen Related Receptor ERR, Homology Modeling, Ligand-Binding Domain, Orphan Nuclear Receptor |
| Abstract | 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. |
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