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  • Title: The binding and activation of the Clr-Cls subunit of the first component of human complement.
    Author: Hughes-Jones NC, Gorick BD.
    Journal: Mol Immunol; 1982 Sep; 19(9):1105-12. PubMed ID: 6292705.
    Abstract:
    The value of the functional affinity constant between 125I-labelled Clq and the Clr-Cls tetramer (when free in solution) in the formation of Cl was found to be 3.6 X 10(7) M-1. When Clq was bound to activating immune complexes, the value of K was about 10-fold higher before initiation of activation and there was a further two to three-fold rise as activation proceeded. The addition of an excess of unlabelled Clq increased the rate of activation of 125I-labelled Cl, suggesting an interaction between Clr-Cls and two neighbouring Clq molecules. It is suggested that the tetramer Clr-Cls may bind bivalently to Clq when free in solution, but on binding to activating complexes, one of the Clr-Cls binding sites is detached from Clq and becomes bound to a site on the complex. The resultant spatial rearrangement of the Clr molecules within the tetramer may be optimal for autocatalytic activation of Clr.
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