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Factor H dimers by Sedimentation Velocity

Factor H dimers by Sedimentation Velocity
Factor H is a 20-SCR domain plasma protein that is crucial for the regulation of complement activation in innate immunity by assisting the degradation of C3b.  The first five short complement regulator (SCR-1/5) domains are required for decay acceleration and cofactor activity involving C3b, while the SCR-16/20 domains possess C3b/C3d and heparin binding sites.  Mutations in SCR-16/20 are associated with kidney failure in atypical haemolytic uraemic syndrome.  Sedimentation velocity data identified a monomer-dimer equilibrium in SCR-16/20 using c(s) size-distribution analyses which revealed two peaks as observed.  However, SCR-1/5 behaved as a monomer in its c(s) plots, as seen from the single observed peak.


Publication:  Okemefuna, A.I., Gilbert, H.E., Griggs, K.M., Ormsby, R.J., Gordeon, D.L. & Perkins, S.J. (2008).  The regulatory SCR-1/5 and cell-surface-binding SCR-16/20 fragments of Factor H reveal partially folded-back solution structures and different self-associative properties. J. Mol. Biol. 375, 80-101.