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Functional model of subcomponent C1 of human complement.

V Weiss, C Fauser, J Engel

    Journal of Molecular Biology
    |June 5, 1986
    PubMed
    Summary
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    The study visualizes the structure of human complement C1s and C1r2 subunits, revealing their domain organization. A model of the C1s-C1r2-C1s complex shows C1s at the tips and C1r catalytic domains centrally, aiding complement activation understanding.

    Area of Science:

    • Immunology
    • Structural Biology
    • Protein Biochemistry

    Background:

    • The first component of human complement (C1) is crucial for the classical activation pathway.
    • Understanding the structural organization of C1 subunits (C1q, C1r, C1s) is essential for deciphering C1 activation mechanisms.
    • Previous structural data on C1r2 and C1s complexes were limited.

    Purpose of the Study:

    • To elucidate the domain organization of human complement C1s and C1r2 subunits.
    • To determine the structural arrangement of the C1s-C1r2-C1s complex.
    • To propose a model for the C1 complex and its activation mechanism.

    Main Methods:

    • Electron microscopy was employed to visualize monomeric C1s, C1r2 dimer, and the C1s-C1r2-C1s complex.
    • Affinity-labeling with biotin and visualization of avidin-ferritin conjugates were used to map C1s positions.

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  • Structural comparisons with C1r fragments aided in domain assignment.

    • Main Results:

    • Monomeric C1s presented as a dumb-bell shape with two globular domains (light and heavy chains) connected by a rod.
    • C1r2 formed an asymmetrical X-shaped dimer with inner catalytic B-chains and outer domains.
    • The C1s-C1r2-C1s complex (54 nm) revealed C1r2 centrally and C1s monomers at the outer tips, with C1s heavy chains interacting with C1r.

    Conclusions:

    • A detailed model of the C1s-C1r2-C1s complex was proposed, placing catalytic domains centrally (C1r) and peripherally (C1s).
    • This structural arrangement provides insights into the spatial positioning of active sites for complement activation.
    • The derived model of the C1 complex aids in understanding the initial steps of the classical complement pathway.