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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Main 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
Format:	Article
Language:	English
Published:	Nature Publishing Group 2018-10-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-018-06632-0

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spelling	doaj-d8f1227aa2394ee08a80e9812006d6b22021-05-11T09:34:15ZengNature Publishing GroupNature Communications2041-17232018-10-019111710.1038/s41467-018-06632-0The architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomersLaura C. Zanetti-Domingues0Dimitrios Korovesis1Sarah R. Needham2Christopher J. Tynan3Shiori Sagawa4Selene K. Roberts5Antonija Kuzmanic6Elena Ortiz-Zapater7Purvi Jain8Rob C. Roovers9Alireza Lajevardipour10Paul M. P. van Bergen en Henegouwen11George Santis12Andrew H. A. Clayton13David T. Clarke14Francesco L. Gervasio15Yibing Shan16David E. Shaw17Daniel J. Rolfe18Peter J. Parker19Marisa L. Martin-Fernandez20Central Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell OxfordCentral Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell OxfordCentral Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell OxfordCentral Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell OxfordD. E. Shaw ResearchCentral Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell OxfordDepartment of Chemistry, Faculty of Maths & Physical Sciences, University College LondonPeter Gore Department of Immunobiology, School of Immunology & Microbial Sciences, Kings College LondonDivision of Cell Biology, Science Faculty, Department of Biology, Utrecht UniversityMerus, LSICentre for Micro-Photonics, Faculty of Science, Engineering and Technology, Swinburne University of TechnologyDivision of Cell Biology, Science Faculty, Department of Biology, Utrecht UniversityPeter Gore Department of Immunobiology, School of Immunology & Microbial Sciences, Kings College LondonCentre for Micro-Photonics, Faculty of Science, Engineering and Technology, Swinburne University of TechnologyCentral Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell OxfordDepartment of Chemistry, Faculty of Maths & Physical Sciences, University College LondonD. E. Shaw ResearchD. E. Shaw ResearchCentral Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell OxfordProtein Phosphorylation Laboratory, The Francis Crick InstituteCentral Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell OxfordTo 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.https://doi.org/10.1038/s41467-018-06632-0
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	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
spellingShingle	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 The architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers Nature Communications
author_facet	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
author_sort	Laura C. Zanetti-Domingues
title	The architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers
title_short	The architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers
title_full	The architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers
title_fullStr	The architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers
title_full_unstemmed	The architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers
title_sort	architecture of egfr’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2018-10-01
description	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.
url	https://doi.org/10.1038/s41467-018-06632-0
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The architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers

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