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Our data favors a model in which PIC1 derivatives functionally disrupt the C1s-C1r-C1r-C1s/MASP interaction with the CLR of C1q/MBL, respectively. By PIC1 binding to the serine protease interaction site on CLR, the serine proteases are hypothesized to be in a suboptimal conformation for autoactivation and initiation of the classical and/or lectin pathways of complement.
