The structure of complement C3b provides insights into complement activation and regulation

A. Abdul Ajees, K. Gunasekaran, John E. Volanakis, Sthanam. V. L. Narayana, Girish J. Kotwal and H. M. Krishna Murthy ()
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A. Abdul Ajees: Center for Biophysical Sciences and Engineering
K. Gunasekaran: Center for Biophysical Sciences and Engineering
John E. Volanakis: Department of Medicine
Sthanam. V. L. Narayana: Center for Biophysical Sciences and Engineering
Girish J. Kotwal: University of Cape Town, HSC
H. M. Krishna Murthy: Center for Biophysical Sciences and Engineering

Nature, 2006, vol. 444, issue 7116, 221-225

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/nature05258

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