Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy

The Src-homology 3 domain of phosphatidyl-inositol-3-kinase (PI3K-SH3) is a model system for studying amyloid fibril formation. Here the authors present the 3.4 Å cryo-EM structure of the PI3K-SH3 amyloid fibril, which allows them to rationalize the effects of mutations on the kinetics of fibril for...

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Autores principales:	Christine Röder, Nicola Vettore, Lena N. Mangels, Lothar Gremer, Raimond B. G. Ravelli, Dieter Willbold, Wolfgang Hoyer, Alexander K. Buell, Gunnar F. Schröder
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/0f72582fb3cd4c3f93c5943eddda0b9c
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spelling	oai:doaj.org-article:0f72582fb3cd4c3f93c5943eddda0b9c2021-12-02T17:01:36ZAtomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy10.1038/s41467-019-11320-82041-1723https://doaj.org/article/0f72582fb3cd4c3f93c5943eddda0b9c2019-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11320-8https://doaj.org/toc/2041-1723The Src-homology 3 domain of phosphatidyl-inositol-3-kinase (PI3K-SH3) is a model system for studying amyloid fibril formation. Here the authors present the 3.4 Å cryo-EM structure of the PI3K-SH3 amyloid fibril, which allows them to rationalize the effects of mutations on the kinetics of fibril formation.Christine RöderNicola VettoreLena N. MangelsLothar GremerRaimond B. G. RavelliDieter WillboldWolfgang HoyerAlexander K. BuellGunnar F. SchröderNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-9 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Christine Röder Nicola Vettore Lena N. Mangels Lothar Gremer Raimond B. G. Ravelli Dieter Willbold Wolfgang Hoyer Alexander K. Buell Gunnar F. Schröder Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy
description	The Src-homology 3 domain of phosphatidyl-inositol-3-kinase (PI3K-SH3) is a model system for studying amyloid fibril formation. Here the authors present the 3.4 Å cryo-EM structure of the PI3K-SH3 amyloid fibril, which allows them to rationalize the effects of mutations on the kinetics of fibril formation.
format	article
author	Christine Röder Nicola Vettore Lena N. Mangels Lothar Gremer Raimond B. G. Ravelli Dieter Willbold Wolfgang Hoyer Alexander K. Buell Gunnar F. Schröder
author_facet	Christine Röder Nicola Vettore Lena N. Mangels Lothar Gremer Raimond B. G. Ravelli Dieter Willbold Wolfgang Hoyer Alexander K. Buell Gunnar F. Schröder
author_sort	Christine Röder
title	Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy
title_short	Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy
title_full	Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy
title_fullStr	Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy
title_full_unstemmed	Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy
title_sort	atomic structure of pi3-kinase sh3 amyloid fibrils by cryo-electron microscopy
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/0f72582fb3cd4c3f93c5943eddda0b9c
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_version_	1718382068416643072

Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy

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