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

Authors :
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
Source :
Nature Communications, Vol 9, Iss 1, Pp 1-17 (2018)
Publication Year :
2018
Publisher :
Nature Portfolio, 2018.

Abstract

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.

Subjects

Subjects :
Science

Details

Language :
English
ISSN :
20411723
Volume :
9
Issue :
1
Database :
Directory of Open Access Journals
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
edsdoj.8f1227aa2394ee08a80e9812006d6b2
Document Type :
article
Full Text :
https://doi.org/10.1038/s41467-018-06632-0