[HTML][HTML] Each of the three binding sites on complement factor H interacts with a distinct site on C3b
TS Jokiranta, J Hellwage, V Koistinen, PF Zipfel… - Journal of Biological …, 2000 - ASBMB
Factor H (fH) restricts activation of the alternative pathway of complement at the level of C3,
both in the fluid phase and on self-structures, but allows the activation to proceed on foreign
structures. To study the interactions between fH and C3b we used surface plasmon
resonance analysis (Biacore®) and eight recombinantly expressed fH constructs containing
fragments of the 20 short consensus repeat domains (SCRs) of fH. We analyzed the binding
of these constructs to C3b and its cleavage products C3c and C3d. Three binding sites for …
both in the fluid phase and on self-structures, but allows the activation to proceed on foreign
structures. To study the interactions between fH and C3b we used surface plasmon
resonance analysis (Biacore®) and eight recombinantly expressed fH constructs containing
fragments of the 20 short consensus repeat domains (SCRs) of fH. We analyzed the binding
of these constructs to C3b and its cleavage products C3c and C3d. Three binding sites for …