Nature Communications (Oct 2018)
The architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers
- 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
Affiliations
- Laura C. Zanetti-Domingues
- Central Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell Oxford
- Dimitrios Korovesis
- Central Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell Oxford
- Sarah R. Needham
- Central Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell Oxford
- Christopher J. Tynan
- Central Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell Oxford
- Shiori Sagawa
- D. E. Shaw Research
- Selene K. Roberts
- Central Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell Oxford
- Antonija Kuzmanic
- Department of Chemistry, Faculty of Maths & Physical Sciences, University College London
- Elena Ortiz-Zapater
- Peter Gore Department of Immunobiology, School of Immunology & Microbial Sciences, Kings College London
- Purvi Jain
- Division of Cell Biology, Science Faculty, Department of Biology, Utrecht University
- Rob C. Roovers
- Merus, LSI
- Alireza Lajevardipour
- Centre for Micro-Photonics, Faculty of Science, Engineering and Technology, Swinburne University of Technology
- Paul M. P. van Bergen en Henegouwen
- Division of Cell Biology, Science Faculty, Department of Biology, Utrecht University
- George Santis
- Peter Gore Department of Immunobiology, School of Immunology & Microbial Sciences, Kings College London
- Andrew H. A. Clayton
- Centre for Micro-Photonics, Faculty of Science, Engineering and Technology, Swinburne University of Technology
- David T. Clarke
- Central Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell Oxford
- Francesco L. Gervasio
- Department of Chemistry, Faculty of Maths & Physical Sciences, University College London
- Yibing Shan
- D. E. Shaw Research
- David E. Shaw
- D. E. Shaw Research
- Daniel J. Rolfe
- Central Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell Oxford
- Peter J. Parker
- Protein Phosphorylation Laboratory, The Francis Crick Institute
- Marisa L. Martin-Fernandez
- Central Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell Oxford
- DOI
- https://doi.org/10.1038/s41467-018-06632-0
- Journal volume & issue
-
Vol. 9,
no. 1
pp. 1 – 17
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.
