Molecular basis of IRGB10 oligomerization and membrane association for pathogen membrane disruption

Ha et al. present a crystal structure of mouse IRGB10, a mouse interferon-inducible GTPase that mediates bacteriolysis in cell autonomous immunity. With further mutagenesis studies, they show that IRGB10 bound to GDP forms an inactive head-to-head dimer, which changes its conformation to activate it...

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Autores principales: Hyun Ji Ha, Hye Lin Chun, So Yeon Lee, Jae-Hee Jeong, Yeon-Gil Kim, Hyun Ho Park
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/ff265e0c1fcd4646bb457b6220dcd6a4
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spelling oai:doaj.org-article:ff265e0c1fcd4646bb457b6220dcd6a42021-12-02T10:49:10ZMolecular basis of IRGB10 oligomerization and membrane association for pathogen membrane disruption10.1038/s42003-020-01640-72399-3642https://doaj.org/article/ff265e0c1fcd4646bb457b6220dcd6a42021-01-01T00:00:00Zhttps://doi.org/10.1038/s42003-020-01640-7https://doaj.org/toc/2399-3642Ha et al. present a crystal structure of mouse IRGB10, a mouse interferon-inducible GTPase that mediates bacteriolysis in cell autonomous immunity. With further mutagenesis studies, they show that IRGB10 bound to GDP forms an inactive head-to-head dimer, which changes its conformation to activate its membrane-binding and disruptive functions.Hyun Ji HaHye Lin ChunSo Yeon LeeJae-Hee JeongYeon-Gil KimHyun Ho ParkNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-10 (2021)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Hyun Ji Ha
Hye Lin Chun
So Yeon Lee
Jae-Hee Jeong
Yeon-Gil Kim
Hyun Ho Park
Molecular basis of IRGB10 oligomerization and membrane association for pathogen membrane disruption
description Ha et al. present a crystal structure of mouse IRGB10, a mouse interferon-inducible GTPase that mediates bacteriolysis in cell autonomous immunity. With further mutagenesis studies, they show that IRGB10 bound to GDP forms an inactive head-to-head dimer, which changes its conformation to activate its membrane-binding and disruptive functions.
format article
author Hyun Ji Ha
Hye Lin Chun
So Yeon Lee
Jae-Hee Jeong
Yeon-Gil Kim
Hyun Ho Park
author_facet Hyun Ji Ha
Hye Lin Chun
So Yeon Lee
Jae-Hee Jeong
Yeon-Gil Kim
Hyun Ho Park
author_sort Hyun Ji Ha
title Molecular basis of IRGB10 oligomerization and membrane association for pathogen membrane disruption
title_short Molecular basis of IRGB10 oligomerization and membrane association for pathogen membrane disruption
title_full Molecular basis of IRGB10 oligomerization and membrane association for pathogen membrane disruption
title_fullStr Molecular basis of IRGB10 oligomerization and membrane association for pathogen membrane disruption
title_full_unstemmed Molecular basis of IRGB10 oligomerization and membrane association for pathogen membrane disruption
title_sort molecular basis of irgb10 oligomerization and membrane association for pathogen membrane disruption
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/ff265e0c1fcd4646bb457b6220dcd6a4
work_keys_str_mv AT hyunjiha molecularbasisofirgb10oligomerizationandmembraneassociationforpathogenmembranedisruption
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AT soyeonlee molecularbasisofirgb10oligomerizationandmembraneassociationforpathogenmembranedisruption
AT jaeheejeong molecularbasisofirgb10oligomerizationandmembraneassociationforpathogenmembranedisruption
AT yeongilkim molecularbasisofirgb10oligomerizationandmembraneassociationforpathogenmembranedisruption
AT hyunhopark molecularbasisofirgb10oligomerizationandmembraneassociationforpathogenmembranedisruption
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