Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations.

ABSTRACT: The human epidermal growth factor receptor (HER) tyrosine kinases homo- and heterodimerize to activate downstream signaling pathways. HER3 is a catalytically impaired member of the HER family that contributes to the development of several human malignancies and is mutated in a subset of cancers. HER3 signaling depends on heterodimerization with a catalytically active partner, in particular epidermal growth factor receptor (EGFR) (the founding family member, also known as HER1) or HER2. The activity of homodimeric complexes of catalytically active HER family members depends on allosteric activation between the two kinase domains. To determine the structural basis for HER3 signaling through heterodimerization with a catalytically active HER family member, we solved the crystal structure of t

SUBMITTER: Littlefield P 

PROVIDER: S-EPMC4492339 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature