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Solution structure of epiregulin and the effect of its C‐terminal domain for receptor binding affinity
Author(s) -
Sato Katsuharu,
Nakamura Takashi,
Mizuguchi Mineyuki,
Miura Kazunori,
Tada Masahito,
Aizawa Tomoyasu,
Gomi Tomoharu,
Miyamoto Kaoru,
Kawano Keiichi
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01005-6
Subject(s) - epiregulin , electron paramagnetic resonance , chemistry , receptor , ligand (biochemistry) , egf like domain , hydrogen bond , epidermal growth factor , crystallography , biophysics , binding domain , binding site , biochemistry , molecule , biology , nuclear magnetic resonance , amphiregulin , physics , organic chemistry
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.