Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites

C-reactive protein is a pentameric protein secreted by the liver in response to injury and infection. Here Braiget al. show that conformational changes in CRP on the surface of monocyte-derived microvesicles enable binding of complement C1q and lead to activation of the complement cascade and aggrav...

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Autores principales:	David Braig, Tracy L. Nero, Hans-Georg Koch, Benedict Kaiser, Xiaowei Wang, Jan R. Thiele, Craig J. Morton, Johannes Zeller, Jurij Kiefer, Lawrence A. Potempa, Natalie A. Mellett, Luke A. Miles, Xiao-Jun Du, Peter J. Meikle, Markus Huber-Lang, G. Björn Stark, Michael W. Parker, Karlheinz Peter, Steffen U. Eisenhardt
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/128f34d5a0f648b598b01c6bc5aab5a5
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spelling	oai:doaj.org-article:128f34d5a0f648b598b01c6bc5aab5a52021-12-02T14:42:18ZTransitional changes in the CRP structure lead to the exposure of proinflammatory binding sites10.1038/ncomms141882041-1723https://doaj.org/article/128f34d5a0f648b598b01c6bc5aab5a52017-01-01T00:00:00Zhttps://doi.org/10.1038/ncomms14188https://doaj.org/toc/2041-1723C-reactive protein is a pentameric protein secreted by the liver in response to injury and infection. Here Braiget al. show that conformational changes in CRP on the surface of monocyte-derived microvesicles enable binding of complement C1q and lead to activation of the complement cascade and aggravation of inflammation.David BraigTracy L. NeroHans-Georg KochBenedict KaiserXiaowei WangJan R. ThieleCraig J. MortonJohannes ZellerJurij KieferLawrence A. PotempaNatalie A. MellettLuke A. MilesXiao-Jun DuPeter J. MeikleMarkus Huber-LangG. Björn StarkMichael W. ParkerKarlheinz PeterSteffen U. EisenhardtNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-19 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q David Braig Tracy L. Nero Hans-Georg Koch Benedict Kaiser Xiaowei Wang Jan R. Thiele Craig J. Morton Johannes Zeller Jurij Kiefer Lawrence A. Potempa Natalie A. Mellett Luke A. Miles Xiao-Jun Du Peter J. Meikle Markus Huber-Lang G. Björn Stark Michael W. Parker Karlheinz Peter Steffen U. Eisenhardt Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites
description	C-reactive protein is a pentameric protein secreted by the liver in response to injury and infection. Here Braiget al. show that conformational changes in CRP on the surface of monocyte-derived microvesicles enable binding of complement C1q and lead to activation of the complement cascade and aggravation of inflammation.
format	article
author	David Braig Tracy L. Nero Hans-Georg Koch Benedict Kaiser Xiaowei Wang Jan R. Thiele Craig J. Morton Johannes Zeller Jurij Kiefer Lawrence A. Potempa Natalie A. Mellett Luke A. Miles Xiao-Jun Du Peter J. Meikle Markus Huber-Lang G. Björn Stark Michael W. Parker Karlheinz Peter Steffen U. Eisenhardt
author_facet	David Braig Tracy L. Nero Hans-Georg Koch Benedict Kaiser Xiaowei Wang Jan R. Thiele Craig J. Morton Johannes Zeller Jurij Kiefer Lawrence A. Potempa Natalie A. Mellett Luke A. Miles Xiao-Jun Du Peter J. Meikle Markus Huber-Lang G. Björn Stark Michael W. Parker Karlheinz Peter Steffen U. Eisenhardt
author_sort	David Braig
title	Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites
title_short	Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites
title_full	Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites
title_fullStr	Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites
title_full_unstemmed	Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites
title_sort	transitional changes in the crp structure lead to the exposure of proinflammatory binding sites
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/128f34d5a0f648b598b01c6bc5aab5a5
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Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites

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