In Factor H, if there are at least two different self-dimerisation sites at SCR-6/8 and SCR-16/20, this leads to the prediction that the two dimer sites would lead to the formation of indefinite Factor H oligomers through the daisy-chaining of these dimer sites. The presence of Factor H dimers and smaller amounts of larger species ranging up to heptamers as well as monomers were confirmed by size-distribution analyses c(s) of ultracentrifugation sedimentation velocity experiments. A series of peaks 2-7 in the c(s) plot were seen as the FH concentration increased.
Publications: Nan, R., Gor, J. & Perkins, S.J. (2008). Implications of the progressive self-association of wild-type human Factor H for complement regulation and disease. J. Mol. Biol. 375, 891-900
Okemefuna, A.I., Nan, R., Gor, J. & Perkins, S.J. (2009). Electrostatic interactions contribute to the folded-back conformation of wild-type human Factor H. J.Mol.Biol. 391, 98-118