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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2017-01-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/ncomms14188 |
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doaj-128f34d5a0f648b598b01c6bc5aab5a52021-05-11T07:15:51ZengNature Publishing GroupNature Communications2041-17232017-01-018111910.1038/ncomms14188Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sitesDavid Braig0Tracy L. Nero1Hans-Georg Koch2Benedict Kaiser3Xiaowei Wang4Jan R. Thiele5Craig J. Morton6Johannes Zeller7Jurij Kiefer8Lawrence A. Potempa9Natalie A. Mellett10Luke A. Miles11Xiao-Jun Du12Peter J. Meikle13Markus Huber-Lang14G. Björn Stark15Michael W. Parker16Karlheinz Peter17Steffen U. Eisenhardt18Department of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of FreiburgACRF Rational Drug Discovery Centre, St Vincent’s Institute of Medical ResearchInstitute for Biochemistry and Molecular Biology and Spemann-Graduate School for Biology and Medicine University of Freiburg, Medical Faculty of the University of FreiburgDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of FreiburgBaker IDI Heart and Diabetes InstituteDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of FreiburgACRF Rational Drug Discovery Centre, St Vincent’s Institute of Medical ResearchDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of FreiburgDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of FreiburgCollege of Pharmacy, Roosevelt UniversityBaker IDI Heart and Diabetes InstituteACRF Rational Drug Discovery Centre, St Vincent’s Institute of Medical ResearchBaker IDI Heart and Diabetes InstituteBaker IDI Heart and Diabetes InstituteDepartment of Traumatology, Hand, Plastic, and Reconstructive Surgery, Center of Surgery, University of UlmDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of FreiburgACRF Rational Drug Discovery Centre, St Vincent’s Institute of Medical ResearchBaker IDI Heart and Diabetes InstituteDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of FreiburgC-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.https://doi.org/10.1038/ncomms14188 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
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 |
spellingShingle |
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 Nature Communications |
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 Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2017-01-01 |
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. |
url |
https://doi.org/10.1038/ncomms14188 |
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