Hydrodynamic data show that C1̄ inhibitor of complement forms compact complexes with C1̄r and C1̄s

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Abstract
The C1̄ inhibitor of the complement cascade forms stoichiometric complexes with C1̄r and C1̄s and controls the activation of first component C1 of complement. Literature sedimentation coefficients s°20.w for the complexes formed between C1̄ inhibitor, C1̄r and C1̄s were analysed using frictional ratios and the hydrodynamic sphere approach. A head‐and‐tail two‐domain model for C1 inhibitor was combined with cylindrical hydrodynamic models for the six‐domain structures of C1̄r and C1̄s. The hydrodynamic data show that the heavily glycosylated N‐terminal domain of C1̄ inhibitor is positioned close to the two complement ‘short consensus repeat’ domains found in the centre of C1̄r and C1̄s.