Rational Design for the Development of Epidermal Growth Factor Receptor Antagonists

Epidermal growth factor (EGF) and transforming growth factor-α (TGFα) bind with similar high affinity to the human EGF receptor. Using a domain-exchange strategy we have shown that the C-terminal linear region of these molecules is involved in high affinity receptor binding. By further single amino...

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Published inPathology, research and practice Vol. 192; no. 7; pp. 761 - 767
Main Authors Van Zoelen, E.J.J., Lenferink, A.E.G., Kramer, R.H., Van De Poll, M.L.M.
Format Journal Article
LanguageEnglish
Published Germany Elsevier GmbH 01.07.1996
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Summary:Epidermal growth factor (EGF) and transforming growth factor-α (TGFα) bind with similar high affinity to the human EGF receptor. Using a domain-exchange strategy we have shown that the C-terminal linear region of these molecules is involved in high affinity receptor binding. By further single amino acid substition in this linear C-terminal region, a putative interaction site of these ligands with their receptor has been identified. This identification of a receptor binding domain in EGF/TGFα provides an important initial step in the development of EGF receptor antagonists with significant clinical potential.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
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ISSN:0344-0338
1618-0631
DOI:10.1016/S0344-0338(96)80098-7