Mechanisms for kinase-mediated dimerization of the epidermal growth factor receptor.

doi:10.1074/jbc.M112.414391

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Article

Mechanisms for kinase-mediated dimerization of the epidermal growth factor receptor.

The Journal of biological chemistry - 2 Nov 2012

Lu Chafen, Mi Li-Zhi, Schürpf Thomas, Walz Thomas, Springer Timothy A

Abstract excerpt

We study a mechanism by which dimerization of the EGF receptor (EGFR) cytoplasmic domain is transmitted to the ectodomain. Therapeutic and other small molecule antagonists to the kinase domain that stabilize its active conformation, but not those that stabilize an inactive conformation, stabilize ectodomain dimerization. Inhibitor-induced dimerization requires an asymmetric kinase domain interface associated with...

Topics

Animals
Binding Sites
Blotting, Western
Cell Line
Cross-Linking Reagents
Disulfides
Epidermal Growth Factor
ErbB Receptors
Gefitinib
Humans
Microscopy, Electron

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Phosphotransferases

Protein Conformation

Protein Kinase Inhibitors

Protein Multimerization

Protein Structure, Tertiary

Quinazolines

Source

Open in PubMed Open full text

Identifiers

PMID: 22988250
DOI: 10.1074/jbc.M112.414391
PMCID: PMC3488093

Genes

EGFR
EGF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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