Conformational analysis of the phosphorylated epidermal growth factor receptor

Phosphorylation-induced conformational changes have been well documented wi th different receptor tyrosine kinases. However, the susceptible epitopes a nd the tyrosine residue(s) involved in particular structural alteration mos tly remain to be determined. Using a conformation-specific anti-peptide ant ibody, we have not only identified one such domain in the C-terminal tail o f the EGF receptor but also identified the phosphate acceptor sites that ar e involved in the conformational change.