Structure of C3b in complex with CRIg gives insights into regulation of complement activation

Christian Wiesmann, Kenneth J. Katschke, JianPing Yin, Karim Y. Helmy, Micah Steffek, Wayne J. Fairbrother, Scott A. McCallum, Lizette Embuscado, Laura DeForge, Philip E. Hass and Menno van Lookeren Campagne ()
Additional contact information
Christian Wiesmann: Department of Protein Engineering
Kenneth J. Katschke: Department of Immunology
JianPing Yin: Department of Protein Engineering
Karim Y. Helmy: Department of Immunology
Micah Steffek: Department of Protein Chemistry
Wayne J. Fairbrother: Department of Protein Engineering
Scott A. McCallum: Department of Protein Engineering
Lizette Embuscado: Department of Assay Technology
Laura DeForge: Department of Assay Technology
Philip E. Hass: Department of Protein Chemistry
Menno van Lookeren Campagne: Department of Immunology

Nature, 2006, vol. 444, issue 7116, 217-220

Abstract: Fishing for complement Three papers in this issue report the first X-ray structures of C3b, the active form of human complement C3. The complement system is a family of blood serum proteins and cell-surface receptors that recognizes pathogens and unleashes the immune response against them. The powerhouse of the C3 protein is a thioester group: when activated it binds to an acceptor on the pathogen and marks it for destruction. There are similar thioesters in host cells too, so the C3 thioester has to be kept tightly under wraps. Knowledge of the structure of the active form of C3b is a step towards designing therapies to manipulate the complement system. Inappropriate activation of the complement system has been implicated in various diseases including arthritis, asthma, lupus erythematosus, autoimmune heart disease and multiple sclerosis.

Date: 2006
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DOI: 10.1038/nature05263

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