Structure of C3b reveals conformational changes that underlie complement activity

Bert J. C. Janssen, Agni Christodoulidou, Andrew McCarthy, John D. Lambris and Piet Gros ()
Additional contact information
Bert J. C. Janssen: Utrecht University
Agni Christodoulidou: University of Pennsylvania
Andrew McCarthy: Grenoble Outstation
John D. Lambris: University of Pennsylvania
Piet Gros: Utrecht University

Nature, 2006, vol. 444, issue 7116, 213-216

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/nature05172

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