Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity

Katsuharu Sato; Takashi Nakamura; Mineyuki Mizuguchi; Kazunori Miura; Masahito Tada; Tomoyasu Aizawa; Tomoharu Gomi; Kaoru Miyamoto; Keiichi Kawano

doi:10.1016/S0014-5793(03)01005-6

Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity

Katsuharu Sato, Takashi Nakamura, Mineyuki Mizuguchi, Kazunori Miura, Masahito Tada, Tomoyasu Aizawa, Tomoharu Gomi, Kaoru Miyamoto, Keiichi Kawano^*

^*Corresponding author for this work

Structural Biology

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

Abstract

Epiregulin (EPR), a novel member of epidermal growth factor (EGF) family, is a ligand for ErbB-1 and ErbB-4 receptors. The binding affinity of EPR for the receptors is lower than those of other EGF-family ligands. The solution structure of EPR was determined using two-dimensional nuclear magnetic resonance spectroscopy. The secondary structure in the C-terminal domain of EPR is different from other EGF-family ligands because of the lack of hydrogen bonds. The structural difference in the C-terminal domain may provide an explanation for the reduced binding affinity of EPR to the ErbB receptors.

Original language	English
Pages (from-to)	232-238
Number of pages	7
Journal	FEBS Letters
Volume	553
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(03)01005-6
State	Published - 2003/10/23

Keywords

Epidermal growth factor
Epiregulin
Nuclear magnetic resonance
Structure

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(03)01005-6

Cite this

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title = "Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity",

abstract = "Epiregulin (EPR), a novel member of epidermal growth factor (EGF) family, is a ligand for ErbB-1 and ErbB-4 receptors. The binding affinity of EPR for the receptors is lower than those of other EGF-family ligands. The solution structure of EPR was determined using two-dimensional nuclear magnetic resonance spectroscopy. The secondary structure in the C-terminal domain of EPR is different from other EGF-family ligands because of the lack of hydrogen bonds. The structural difference in the C-terminal domain may provide an explanation for the reduced binding affinity of EPR to the ErbB receptors.",

keywords = "Epidermal growth factor, Epiregulin, Nuclear magnetic resonance, Structure",

author = "Katsuharu Sato and Takashi Nakamura and Mineyuki Mizuguchi and Kazunori Miura and Masahito Tada and Tomoyasu Aizawa and Tomoharu Gomi and Kaoru Miyamoto and Keiichi Kawano",

note = "Funding Information: This work was supported by grants from the Program for the Promotion of Basic Research Activities for Innovative Biosciences (PROBRAIN) and from the Ministry of Education, Culture, Sports, Science and Technology of Japan to K.K.",

year = "2003",

month = oct,

day = "23",

doi = "10.1016/S0014-5793(03)01005-6",

language = "英語",

volume = "553",

pages = "232--238",

journal = "FEBS Letters",

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publisher = "John Wiley and Sons Inc.",

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TY - JOUR

T1 - Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity

AU - Sato, Katsuharu

AU - Nakamura, Takashi

AU - Mizuguchi, Mineyuki

AU - Miura, Kazunori

AU - Tada, Masahito

AU - Aizawa, Tomoyasu

AU - Gomi, Tomoharu

AU - Miyamoto, Kaoru

AU - Kawano, Keiichi

N1 - Funding Information: This work was supported by grants from the Program for the Promotion of Basic Research Activities for Innovative Biosciences (PROBRAIN) and from the Ministry of Education, Culture, Sports, Science and Technology of Japan to K.K.

PY - 2003/10/23

Y1 - 2003/10/23

N2 - Epiregulin (EPR), a novel member of epidermal growth factor (EGF) family, is a ligand for ErbB-1 and ErbB-4 receptors. The binding affinity of EPR for the receptors is lower than those of other EGF-family ligands. The solution structure of EPR was determined using two-dimensional nuclear magnetic resonance spectroscopy. The secondary structure in the C-terminal domain of EPR is different from other EGF-family ligands because of the lack of hydrogen bonds. The structural difference in the C-terminal domain may provide an explanation for the reduced binding affinity of EPR to the ErbB receptors.

AB - Epiregulin (EPR), a novel member of epidermal growth factor (EGF) family, is a ligand for ErbB-1 and ErbB-4 receptors. The binding affinity of EPR for the receptors is lower than those of other EGF-family ligands. The solution structure of EPR was determined using two-dimensional nuclear magnetic resonance spectroscopy. The secondary structure in the C-terminal domain of EPR is different from other EGF-family ligands because of the lack of hydrogen bonds. The structural difference in the C-terminal domain may provide an explanation for the reduced binding affinity of EPR to the ErbB receptors.

KW - Epidermal growth factor

KW - Epiregulin

KW - Nuclear magnetic resonance

KW - Structure

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U2 - 10.1016/S0014-5793(03)01005-6

DO - 10.1016/S0014-5793(03)01005-6

M3 - 学術論文

C2 - 14572630

AN - SCOPUS:0142200355

SN - 0014-5793

VL - 553

SP - 232

EP - 238

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity

Abstract

Keywords

ASJC Scopus subject areas

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