CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid

hnRNPA2 is involved in RNA metabolism and can form both functional amyloid-like fibrils in membraneless organelles, and pathogenic fibrils in neurodegenerative conditions. Here, the authors present the cryo-EM fibril structure of the wild-type hnRNPA2 low-complexity domain (LCD) and the crystal stru...

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Autores principales:	Jiahui Lu, Qin Cao, Michael P. Hughes, Michael R. Sawaya, David R. Boyer, Duilio Cascio, David S. Eisenberg
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/ebd048782b074d139ebdf2478999499b
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spelling	oai:doaj.org-article:ebd048782b074d139ebdf2478999499b2021-12-02T19:06:29ZCryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid10.1038/s41467-020-17905-y2041-1723https://doaj.org/article/ebd048782b074d139ebdf2478999499b2020-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17905-yhttps://doaj.org/toc/2041-1723hnRNPA2 is involved in RNA metabolism and can form both functional amyloid-like fibrils in membraneless organelles, and pathogenic fibrils in neurodegenerative conditions. Here, the authors present the cryo-EM fibril structure of the wild-type hnRNPA2 low-complexity domain (LCD) and the crystal structure of a LCD segment with the disease causing D290V variant and discuss how mutations can transform fibril structure from a functional to a pathogenic form.Jiahui LuQin CaoMichael P. HughesMichael R. SawayaDavid R. BoyerDuilio CascioDavid S. EisenbergNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jiahui Lu Qin Cao Michael P. Hughes Michael R. Sawaya David R. Boyer Duilio Cascio David S. Eisenberg CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid
description	hnRNPA2 is involved in RNA metabolism and can form both functional amyloid-like fibrils in membraneless organelles, and pathogenic fibrils in neurodegenerative conditions. Here, the authors present the cryo-EM fibril structure of the wild-type hnRNPA2 low-complexity domain (LCD) and the crystal structure of a LCD segment with the disease causing D290V variant and discuss how mutations can transform fibril structure from a functional to a pathogenic form.
format	article
author	Jiahui Lu Qin Cao Michael P. Hughes Michael R. Sawaya David R. Boyer Duilio Cascio David S. Eisenberg
author_facet	Jiahui Lu Qin Cao Michael P. Hughes Michael R. Sawaya David R. Boyer Duilio Cascio David S. Eisenberg
author_sort	Jiahui Lu
title	CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid
title_short	CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid
title_full	CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid
title_fullStr	CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid
title_full_unstemmed	CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid
title_sort	cryoem structure of the low-complexity domain of hnrnpa2 and its conversion to pathogenic amyloid
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/ebd048782b074d139ebdf2478999499b
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CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid

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