The DOI matches its Crossref record; 137 of the 137 references it cites were found in a registry or an index.
A Structural Perspective on the Regulation of the Epidermal Growth Factor Receptor
Open accessAbstract
The epidermal growth factor receptor (EGFR) is a receptor tyrosine kinase that plays a critical role in the pathogenesis of many cancers. The structure of intact forms of this receptor has yet to be determined, but intense investigations of fragments of the receptor have provided a detailed view of its activation mechanism, which we review here. Ligand binding converts the receptor to a dimeric form, in which contacts are restricted to the receptor itself, allowing heterodimerization of the four EGFR family members without direct ligand involvement. Activation of the receptor depends on the formation of an asymmetric dimer of kinase domains, in which one kinase domain allosterically activates the other. Coupling between the extracellular and intracellular domains may involve a switch between alternative crossings of the transmembrane helices, which form dimeric structures. We also discuss how receptor regulation is compromised by oncogenic mutations and the structural basis for negative cooperativity in ligand binding.
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Cites
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Cited by
EGFR in Cancer: Signaling Mechanisms, Drugs, and Acquired Resistance
Uribe, M. L., Marrocco, I., & Yarden, Y. (2021) · Cancers · doi:10.3390/cancers13112748 · Cited by 604
Metadata
- Authors
- Kovacs, E., Zorn, J. A., Huang, Y., Barros, T., & Kuriyan, J.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2015-06-02
- Volume
- 84
- Issue
- 1
- Pages
- 739-764
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2136343696
- Cited by
- 371
- References
- 137
- FWCI
- 3.82
- Type
- journal article
- Language
- en
- Open access
- green
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