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FEBS Lett ; 553(3): 232-8, 2003 Oct 23.
Article in English | MEDLINE | ID: mdl-14572630

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.


Subject(s)
Epidermal Growth Factor/chemistry , Epidermal Growth Factor/metabolism , ErbB Receptors/metabolism , Amino Acid Sequence , Circular Dichroism , Epidermal Growth Factor/genetics , Epiregulin , Escherichia coli/genetics , Escherichia coli/metabolism , Hydrogen Bonding , Models, Molecular , Molecular Sequence Data , Nuclear Magnetic Resonance, Biomolecular , Protein Binding , Protein Structure, Secondary , Protein Structure, Tertiary , Recombinant Fusion Proteins/chemistry , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Sequence Homology, Amino Acid , Solutions/chemistry
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