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

doi:10.4028/0-87849-958-x.107

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 journal › Article › peer-review

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 language	English
Pages (from-to)	107-112
Number of pages	6
Journal	Key Engineering Materials
Volume	277-279
Issue number	I
DOIs	https://doi.org/10.4028/0-87849-958-x.107
Publication status	Published - 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

General Materials Science
Mechanics of Materials
Mechanical Engineering

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10.4028/0-87849-958-x.107

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title = "Structural comparison of ligand-binding domains in estrogen-related receptors",

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

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doi = "10.4028/0-87849-958-x.107",

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AU - Kim, Hye Yeon

AU - Pae, Ae Nim

AU - Lee, Yeon Joo

AU - Park, Joonkyu

AU - Kim, Dae Sung

AU - Hwang, Kwang Yeon

AU - Yu, Myeong Hee

AU - Kim, Eunice Eun Kyeong

PY - 2005

Y1 - 2005

N2 - 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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KW - 4-hydroxyltamoxifen (OHT)

KW - Diethylstilbestrol (DES)

KW - Estrogen receptor (ER)

KW - Estrogen related receptor (ERR)

KW - Homology modeling

KW - Ligand-binding domain

KW - Orphan nuclear receptor

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EP - 112

JO - Key Engineering Materials

JF - Key Engineering Materials

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

Abstract

Keywords

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