Structural comparison of ligand-binding domains in estrogen-related receptors

Authors
Kim, HYPae, ANLee, YJPark, JKim, DSHwang, KYYu, MHKim, EE
Issue Date
2005-01
Publisher
TRANS TECH PUBLICATIONS LTD
Citation
ON THE CONVERGENCE OF BIO-INFORMATION-, ENVIRONMENTAL-, ENERGY-, SPACE- AND NANO-TECHNOLOGIES, PTS 1 AND 2, v.277-279, pp.107 - 112
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.
Keywords
INDEPENDENT TRANSCRIPTIONAL ACTIVATION; ERR; COACTIVATOR; ALPHA-1; GAMMA; BETA; 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
ISSN
1013-9826
URI
https://pubs.kist.re.kr/handle/201004/136876
DOI
10.4028/www.scientific.net/KEM.277-279.107
Appears in Collections:
KIST Article > 2005
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