The cryo-EM structure of the acid activatable pore-forming immune effector Macrophage-expressed gene 1
Macrophage-expressed gene 1 (MPEG1) functions within the phagolysosome to damage engulfed microbes, presumably via forming pores in target membranes. In order to provide insights into the mechanism of MPEG1 function and membrane binding, the authors present structures of hexadecameric MPEG1 prepores...
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Nature Portfolio
2019
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oai:doaj.org-article:2cd82268e003405ba51038290da8f4fe2021-12-02T14:38:37ZThe cryo-EM structure of the acid activatable pore-forming immune effector Macrophage-expressed gene 110.1038/s41467-019-12279-22041-1723https://doaj.org/article/2cd82268e003405ba51038290da8f4fe2019-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-12279-2https://doaj.org/toc/2041-1723Macrophage-expressed gene 1 (MPEG1) functions within the phagolysosome to damage engulfed microbes, presumably via forming pores in target membranes. In order to provide insights into the mechanism of MPEG1 function and membrane binding, the authors present structures of hexadecameric MPEG1 prepores both in solution and in complex with liposomes.Siew Siew PangCharles Bayly-JonesMazdak RadjainiaBradley A. SpicerRuby H. P. LawAdrian W. HodelEdward S. ParsonsSusan M. EkkelPaul J. ConroyGeorg RammHariprasad VenugopalPhillip I. BirdBart W. HoogenboomIlia VoskoboinikYann GambinEmma SiereckiMichelle A. DunstoneJames C. WhisstockNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-9 (2019) |
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Science Q Siew Siew Pang Charles Bayly-Jones Mazdak Radjainia Bradley A. Spicer Ruby H. P. Law Adrian W. Hodel Edward S. Parsons Susan M. Ekkel Paul J. Conroy Georg Ramm Hariprasad Venugopal Phillip I. Bird Bart W. Hoogenboom Ilia Voskoboinik Yann Gambin Emma Sierecki Michelle A. Dunstone James C. Whisstock The cryo-EM structure of the acid activatable pore-forming immune effector Macrophage-expressed gene 1 |
description |
Macrophage-expressed gene 1 (MPEG1) functions within the phagolysosome to damage engulfed microbes, presumably via forming pores in target membranes. In order to provide insights into the mechanism of MPEG1 function and membrane binding, the authors present structures of hexadecameric MPEG1 prepores both in solution and in complex with liposomes. |
format |
article |
author |
Siew Siew Pang Charles Bayly-Jones Mazdak Radjainia Bradley A. Spicer Ruby H. P. Law Adrian W. Hodel Edward S. Parsons Susan M. Ekkel Paul J. Conroy Georg Ramm Hariprasad Venugopal Phillip I. Bird Bart W. Hoogenboom Ilia Voskoboinik Yann Gambin Emma Sierecki Michelle A. Dunstone James C. Whisstock |
author_facet |
Siew Siew Pang Charles Bayly-Jones Mazdak Radjainia Bradley A. Spicer Ruby H. P. Law Adrian W. Hodel Edward S. Parsons Susan M. Ekkel Paul J. Conroy Georg Ramm Hariprasad Venugopal Phillip I. Bird Bart W. Hoogenboom Ilia Voskoboinik Yann Gambin Emma Sierecki Michelle A. Dunstone James C. Whisstock |
author_sort |
Siew Siew Pang |
title |
The cryo-EM structure of the acid activatable pore-forming immune effector Macrophage-expressed gene 1 |
title_short |
The cryo-EM structure of the acid activatable pore-forming immune effector Macrophage-expressed gene 1 |
title_full |
The cryo-EM structure of the acid activatable pore-forming immune effector Macrophage-expressed gene 1 |
title_fullStr |
The cryo-EM structure of the acid activatable pore-forming immune effector Macrophage-expressed gene 1 |
title_full_unstemmed |
The cryo-EM structure of the acid activatable pore-forming immune effector Macrophage-expressed gene 1 |
title_sort |
cryo-em structure of the acid activatable pore-forming immune effector macrophage-expressed gene 1 |
publisher |
Nature Portfolio |
publishDate |
2019 |
url |
https://doaj.org/article/2cd82268e003405ba51038290da8f4fe |
work_keys_str_mv |
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