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

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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Main Authors: 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
Format: article
Language:EN
Published: Nature Portfolio 2017
Subjects:
Science
Q
Online Access:https://doaj.org/article/128f34d5a0f648b598b01c6bc5aab5a5
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Summary: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.

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