Ontology highlight
ABSTRACT:
SUBMITTER: Purba ER
PROVIDER: S-EPMC9748436 | biostudies-literature | 2022
REPOSITORIES: biostudies-literature
Purba Endang R ER Saita Ei-Ichiro EI Akhouri Reetesh R RR Öfverstedt Lars-Goran LG Wilken Gunnar G Skoglund Ulf U Maruyama Ichiro N IN
Frontiers in endocrinology 20221130
Aberrant activation of the epidermal growth factor receptor (EGFR) by mutations has been implicated in a variety of human cancers. Elucidation of the structure of the full-length receptor is essential to understand the molecular mechanisms underlying its activation. Unlike previously anticipated, here, we report that purified full-length EGFR adopts a homodimeric form <i>in vitro</i> before and after ligand binding. Cryo-electron tomography analysis of the purified receptor also showed that the ...[more]