Allosteric Inhibition of the Epidermal Growth Factor Receptor.

ABSTRACT: We previously reported a family of hydrocarbon-stapled peptides designed to interact with the epidermal growth factor receptor (EGFR) juxtamembrane (JM) segment, blocking its ability to form a coiled coil dimer that is essential for receptor activation. These hydrocarbon-stapled peptides, most notably E1^S, decreased the proliferation of cell lines that express wild-type EGFR (H2030 and A431) as well as those expressing the oncogenic mutants EGFR L858R (H3255) and L858R/T790M (H1975). Although our previous investigations provided evidence that E1^S interacted with EGFR directly, the location and details of these interactions were not established. Here we apply biochemical and cross-linking mass spectrometry tools to better define the interactions between E1^S

SUBMITTER: Sinclair JKL 

PROVIDER: S-EPMC8815332 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature