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The structural basis for binding of complement by immunoglobulin M.

M M Hurst, J E Volanakis, R B Hester

    The Journal of Experimental Medicine
    |October 1, 1974
    PubMed
    Summary
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    Researchers identified key structural components of human immunoglobulin M (IgM) responsible for binding complement component 1 (C1). The C(H)4 domain, specifically its amino-terminal region, appears crucial for initiating the complement cascade.

    Area of Science:

    • Immunology
    • Structural Biology
    • Complement System

    Background:

    • Human immunoglobulin M (IgM) is a crucial part of the innate immune system.
    • IgM's ability to activate the complement system is vital for pathogen clearance.
    • Understanding IgM's structure-function relationship in complement activation is essential.

    Purpose of the Study:

    • To identify the specific structural regions of human IgM responsible for binding complement component 1 (C1).
    • To elucidate the molecular mechanisms underlying IgM-mediated complement activation.

    Main Methods:

    • Analysis of human IgM subfragments for their ability to bind active C1.
    • Characterization of the smallest C1-binding fragments, including molecular weight and residue count.

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    Main Results:

    • The major CNBr fragment of the Fc portion of IgM and the C(H)4 fragment were the smallest identified C1-binding fragments.
    • The smallest C1-fixing fragment has a molecular weight of 6,800, comprises 60 residues, and lacks carbohydrate.
    • Structural analysis suggests the amino-terminal 24 residues of the C(H)4 domain are likely responsible for C1 fixation.

    Conclusions:

    • The C(H)4 domain, particularly its amino-terminal portion, plays a critical role in human IgM's ability to initiate complement activation.
    • This finding provides insight into the structural basis of IgM-mediated immunity.