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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Circular Dichroism
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Epidermal Growth Factor / chemistry*
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Epidermal Growth Factor / genetics
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Epidermal Growth Factor / metabolism*
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Epiregulin
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ErbB Receptors / metabolism*
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Hydrogen Bonding
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Models, Molecular
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular
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Protein Binding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Sequence Homology, Amino Acid
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Solutions / chemistry
Substances
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Epiregulin
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Recombinant Fusion Proteins
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Solutions
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Epidermal Growth Factor
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ErbB Receptors