Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation

The SRP Alu domain is involved in co-translational protein targeting. Soni et al. investigate the Alu domain of Plasmodium falciparum, the agent of malaria, and find that unlike any other it adopts an open conformation.

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Autores principales: Komal Soni, Georg Kempf, Karen Manalastas-Cantos, Astrid Hendricks, Dirk Flemming, Julien Guizetti, Bernd Simon, Friedrich Frischknecht, Dmitri I. Svergun, Klemens Wild, Irmgard Sinning
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/209bda6b89384eceb72f2290525335c3
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spelling oai:doaj.org-article:209bda6b89384eceb72f2290525335c32021-12-02T15:52:54ZStructural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation10.1038/s42003-021-02132-y2399-3642https://doaj.org/article/209bda6b89384eceb72f2290525335c32021-05-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02132-yhttps://doaj.org/toc/2399-3642The SRP Alu domain is involved in co-translational protein targeting. Soni et al. investigate the Alu domain of Plasmodium falciparum, the agent of malaria, and find that unlike any other it adopts an open conformation.Komal SoniGeorg KempfKaren Manalastas-CantosAstrid HendricksDirk FlemmingJulien GuizettiBernd SimonFriedrich FrischknechtDmitri I. SvergunKlemens WildIrmgard SinningNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-14 (2021)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Komal Soni
Georg Kempf
Karen Manalastas-Cantos
Astrid Hendricks
Dirk Flemming
Julien Guizetti
Bernd Simon
Friedrich Frischknecht
Dmitri I. Svergun
Klemens Wild
Irmgard Sinning
Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation
description The SRP Alu domain is involved in co-translational protein targeting. Soni et al. investigate the Alu domain of Plasmodium falciparum, the agent of malaria, and find that unlike any other it adopts an open conformation.
format article
author Komal Soni
Georg Kempf
Karen Manalastas-Cantos
Astrid Hendricks
Dirk Flemming
Julien Guizetti
Bernd Simon
Friedrich Frischknecht
Dmitri I. Svergun
Klemens Wild
Irmgard Sinning
author_facet Komal Soni
Georg Kempf
Karen Manalastas-Cantos
Astrid Hendricks
Dirk Flemming
Julien Guizetti
Bernd Simon
Friedrich Frischknecht
Dmitri I. Svergun
Klemens Wild
Irmgard Sinning
author_sort Komal Soni
title Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation
title_short Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation
title_full Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation
title_fullStr Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation
title_full_unstemmed Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation
title_sort structural analysis of the srp alu domain from plasmodium falciparum reveals a non-canonical open conformation
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/209bda6b89384eceb72f2290525335c3
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