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Publication Detail
Hydrodynamic data show that C1̄ inhibitor of complement forms compact complexes with C1̄r and C1̄s
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Perkins SJ
  • Publication date:
  • Pagination:
    89, 92
  • Journal:
    FEBS Letters
  • Volume:
  • Issue:
  • Status:
  • Print ISSN:
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. © 1990.
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