The signalling conformation of the insulin receptor ectodomain

The insulin receptor plays a key role in many physiological processes, yet how insulin effects receptor signaling at the structural level remains incomplete. Here the authors present a high-resolution cryo-EM structure of a high-affinity form of the insulin-bound insulin receptor ectodomain that she...

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Autores principales: Felix Weis, John G. Menting, Mai B. Margetts, Shu Jin Chan, Yibin Xu, Norbert Tennagels, Paulus Wohlfart, Thomas Langer, Christoph W. Müller, Matthias K. Dreyer, Michael C. Lawrence
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Lenguaje:EN
Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/26514aec68da4bd983dcd057a121b978
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spelling oai:doaj.org-article:26514aec68da4bd983dcd057a121b9782021-12-02T17:32:29ZThe signalling conformation of the insulin receptor ectodomain10.1038/s41467-018-06826-62041-1723https://doaj.org/article/26514aec68da4bd983dcd057a121b9782018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06826-6https://doaj.org/toc/2041-1723The insulin receptor plays a key role in many physiological processes, yet how insulin effects receptor signaling at the structural level remains incomplete. Here the authors present a high-resolution cryo-EM structure of a high-affinity form of the insulin-bound insulin receptor ectodomain that sheds light on the mechanism of signal transduction.Felix WeisJohn G. MentingMai B. MargettsShu Jin ChanYibin XuNorbert TennagelsPaulus WohlfartThomas LangerChristoph W. MüllerMatthias K. DreyerMichael C. LawrenceNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Felix Weis
John G. Menting
Mai B. Margetts
Shu Jin Chan
Yibin Xu
Norbert Tennagels
Paulus Wohlfart
Thomas Langer
Christoph W. Müller
Matthias K. Dreyer
Michael C. Lawrence
The signalling conformation of the insulin receptor ectodomain
description The insulin receptor plays a key role in many physiological processes, yet how insulin effects receptor signaling at the structural level remains incomplete. Here the authors present a high-resolution cryo-EM structure of a high-affinity form of the insulin-bound insulin receptor ectodomain that sheds light on the mechanism of signal transduction.
format article
author Felix Weis
John G. Menting
Mai B. Margetts
Shu Jin Chan
Yibin Xu
Norbert Tennagels
Paulus Wohlfart
Thomas Langer
Christoph W. Müller
Matthias K. Dreyer
Michael C. Lawrence
author_facet Felix Weis
John G. Menting
Mai B. Margetts
Shu Jin Chan
Yibin Xu
Norbert Tennagels
Paulus Wohlfart
Thomas Langer
Christoph W. Müller
Matthias K. Dreyer
Michael C. Lawrence
author_sort Felix Weis
title The signalling conformation of the insulin receptor ectodomain
title_short The signalling conformation of the insulin receptor ectodomain
title_full The signalling conformation of the insulin receptor ectodomain
title_fullStr The signalling conformation of the insulin receptor ectodomain
title_full_unstemmed The signalling conformation of the insulin receptor ectodomain
title_sort signalling conformation of the insulin receptor ectodomain
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/26514aec68da4bd983dcd057a121b978
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