ErbB1-4 receptor signaling
Eps-homology (EH) domains are frequently present in proteins involved in the internalization and trafficking of receptors. We determined the structures of the EH1 and EH2 domains of the protein Eps-15, a direct target of the activated ErbB1-4 receptors, identified their Ca2+ binding sites and peptide binding pocket. We also determined the structure of an EGF/TGF chimera and derived a model for its interaction with the extra-cellular ErbB1,3 domains.
Key publications:
■ Whitehead, B., Tessari,
M., Carotenuto, A., Bergen en Henegouwen, P.M.P. van, &
Vuister, G.W. (1999) “The EH1 domain of Eps15 is
structurally classified as a member of the S100 subclass of
EF-hand-containing proteins, Biochemistry 38, 11271-11277.
■ Wingens, M., Walma, T., van Ingen, H., Stortelers,
C., van Leeuwen, J.E.M., van Zoelen, E.J.J. & Vuister,
G.W. (2003) “Structural analysis of an EGF/TGFa
chimera with unique ERBb binding specificity”, J.
Biol. Chem. 278, 39114-39123.