The architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers

The architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers

To prevent ligand-independent dimerisation the epidermal growth factor receptor (EGFR) is autoinhibited by an extracellular dimer interaction. Here, the authors use several imaging technologies and simulations to provide structural insights on the inactive species and on how intracellular mutations...

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Autores principales: Laura C. Zanetti-Domingues, Dimitrios Korovesis, Sarah R. Needham, Christopher J. Tynan, Shiori Sagawa, Selene K. Roberts, Antonija Kuzmanic, Elena Ortiz-Zapater, Purvi Jain, Rob C. Roovers, Alireza Lajevardipour, Paul M. P. van Bergen en Henegouwen, George Santis, Andrew H. A. Clayton, David T. Clarke, Francesco L. Gervasio, Yibing Shan, David E. Shaw, Daniel J. Rolfe, Peter J. Parker, Marisa L. Martin-Fernandez
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2018
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Science
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Acceso en línea:https://doaj.org/article/d8f1227aa2394ee08a80e9812006d6b2
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Sumario:To prevent ligand-independent dimerisation the epidermal growth factor receptor (EGFR) is autoinhibited by an extracellular dimer interaction. Here, the authors use several imaging technologies and simulations to provide structural insights on the inactive species and on how intracellular mutations circumvent the autoinhibition of the basal state.

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