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FH Oligomers by Sedimentation Velocity

FH Oligomers by Sedimentation Velocity
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