Journal article

Epidermal growth factor receptor: Structure-function informing the design of anticancer therapeutics

Ruth A Mitchell, Rodney B Luwor, Antony W Burgess



Research on the epidermal growth factor (EGF) family and the family of receptors (EGFR) has progressed rapidly in recent times. New crystal structures of the ectodomains with different ligands, the activation of the kinase domain through oligomerisation and the use of fluorescence techniques have revealed profound conformational changes on ligand binding. The control of cell signaling from the EGFR-family is complex, with heterodimerisation, ligand affinity and signaling cross-talk influencing cellular outcomes. Analysis of tissue homeostasis indicates that the control of pro-ligand processing is likely to be as important as receptor activation events. Several members of the EGFR-family are ..

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Awarded by National Health and Medical Research Council

Awarded by Victorian Cancer Agency Mid-Career Research Fellowship

Funding Acknowledgements

This work was funded in part by the National Health and Medical Research Council through Program Grant no. 1092788. The granting agency had no direct input into this article. R.B.L. is a recipient of the Victorian Cancer Agency Mid-Career Research Fellowship (MCRF15017). RAM. is a recipient of a Brain Foundation research grant and a Royal Australasian College of Surgeons Research Scholarship.