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. Author manuscript; available in PMC: 2014 May 22.
Published in final edited form as: Nephrology (Carlton). 2010 Oct;15(7):663–675. doi: 10.1111/j.1440-1797.2010.01373.x

Fig. 3.

Fig. 3

Structure and function of Factor H. (A) Schematic representation of fH functional domains. Each SCR is shown as a filled circle. The four N-terminal SCR contain cofactor and decay-accelerating activities while the two C-terminal SCR are primarily responsible for binding to the host cell surface. (B) Factor H is a unique complement regulator as it inhibits AP complement activity in the fluid-phase (1) as well as on the host cell surface (2). Only the cofactor activity of fH is illustrated here.