@article{e9fd1ba3ab6841608a270c7410445888,
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",
issn = "0014-5793",
publisher = "John Wiley and Sons Inc.",
number = "3",
}