Complement regulation at the molecular level: the structure of decay-accelerating factor.
Lukacik P., Roversi P., White J., Esser D., Smith GP., Billington J., Williams PA., Rudd PM., Wormald MR., Harvey DJ., Crispin MD., Radcliffe CM., Dwek RA., Evans DJ., Morgan BP., Smith RA., Lea SM.
The human complement regulator CD55 is a key molecule protecting self-cells from complement-mediated lysis. X-ray diffraction and analytical ultracentrifugation data reveal a rod-like arrangement of four short consensus repeat (SCR) domains in both the crystal and solution. The stalk linking the four SCR domains to the glycosylphosphatidylinositol anchor is extended by the addition of 11 highly charged O-glycans and positions the domains an estimated 177 A above the membrane. Mutation mapping and hydrophobic potential analysis suggest that the interaction with the convertase, and thus complement regulation, depends on the burial of a hydrophobic patch centered on the linker between SCR domains 2 and 3.