 the 
 epidermal growth factor receptor ( egfr ) tyrosine kinase is 
 implicated in a large number of human cancers . 
 most egfr inhibitors 
 target the extracellular , growth factor - binding domain or the intracellular , 
 atp - binding domain . here 
 we describe molecules that inhibit the kinase 
 activity of egfr in a new way , by competing with formation of an essential 
 intradimer coiled coil containing the juxtamembrane segment from each 
 member of the receptor partnership . 
 the most potent molecules we describe 
 bind egfr directly , decrease the proliferation of wild - type and mutant 
 egfr - dependent cells lines , inhibit phosphorylation of egfr and downstream 
 targets , and block coiled coil formation as judged by bipartite tetracysteine 
 display . 
 potency is directly correlated with the ability to block 
 coiled coil formation within full - length egfr in cells . 
Supplementary Material