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

Hye Yeon Kim, Ae Nim Pae, Yeon Joo Lee, Joonkyu Park, Dae Sung Kim, Kwang Yeon Hwang, Myeong Hee Yu, Eunice Eun Kyeong Kim

Research output: Contribution to journalArticle

1 Citation (Scopus)

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.

Original languageEnglish
Pages (from-to)107-112
Number of pages6
JournalKey Engineering Materials
Volume277-279
Issue numberI
DOIs
Publication statusPublished - 2005

Keywords

  • 4-hydroxyltamoxifen (OHT)
  • Diethylstilbestrol (DES)
  • Estrogen receptor (ER)
  • Estrogen related receptor (ERR)
  • Homology modeling
  • Ligand-binding domain
  • Orphan nuclear receptor

ASJC Scopus subject areas

  • Materials Science(all)
  • Mechanics of Materials
  • Mechanical Engineering

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  • Cite this

    Kim, H. Y., Pae, A. N., Lee, Y. J., Park, J., Kim, D. S., Hwang, K. Y., Yu, M. H., & Kim, E. E. K. (2005). Structural comparison of ligand-binding domains in estrogen-related receptors. Key Engineering Materials, 277-279(I), 107-112. https://doi.org/10.4028/0-87849-958-x.107