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...
Saved in:
Published in | Pathology, research and practice Vol. 192; no. 7; pp. 761 - 767 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Germany
Elsevier GmbH
01.07.1996
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
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 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
ISSN: | 0344-0338 1618-0631 |
DOI: | 10.1016/S0344-0338(96)80098-7 |