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
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/d8f1227aa2394ee08a80e9812006d6b2
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spelling	oai:doaj.org-article:d8f1227aa2394ee08a80e9812006d6b22021-12-02T15:34:39ZThe architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers10.1038/s41467-018-06632-02041-1723https://doaj.org/article/d8f1227aa2394ee08a80e9812006d6b22018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06632-0https://doaj.org/toc/2041-1723To 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.Laura C. Zanetti-DominguesDimitrios KorovesisSarah R. NeedhamChristopher J. TynanShiori SagawaSelene K. RobertsAntonija KuzmanicElena Ortiz-ZapaterPurvi JainRob C. RooversAlireza LajevardipourPaul M. P. van Bergen en HenegouwenGeorge SantisAndrew H. A. ClaytonDavid T. ClarkeFrancesco L. GervasioYibing ShanDavid E. ShawDaniel J. RolfePeter J. ParkerMarisa L. Martin-FernandezNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-17 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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
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.
format	article
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
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 Portfolio
publishDate	2018
url	https://doaj.org/article/d8f1227aa2394ee08a80e9812006d6b2
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The architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers

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