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Complete primary structure for the zymogen of human complement factor B.

J E Mole, J K Anderson, E A Davison

    The Journal of Biological Chemistry
    |March 25, 1984
    PubMed
    Summary
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    Complement factor B

    Area of Science:

    • Biochemistry
    • Immunology
    • Proteomics

    Background:

    • Complement factor B (B) is a crucial component of the alternative pathway of the complement system.
    • Understanding its structure and function is vital for comprehending immune responses and developing therapeutic strategies.

    Purpose of the Study:

    • To establish the complete amino acid sequence of complement factor B.
    • To analyze the structural features of its catalytic subunit (Bb) and its relationship to known serine proteases.
    • To investigate potential evolutionary origins and functional implications of unique sequence regions.

    Main Methods:

    • Combined protein and DNA sequencing strategies were employed to determine the full amino acid sequence.
    • Sequence alignment and three-dimensional modeling were used to compare complement factor B with classical serine proteases.

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  • Analysis of internal sequence homology within the Ba fragment was performed.

    • Main Results:

    • The complete 739-amino acid sequence of complement factor B was elucidated, revealing four N-linked glycosylation sites.
    • The catalytic Bb subunit (259 amino acids) exhibits unique structural features distinct from classical serine proteases.
    • The Ba fragment contains novel homologous regions, suggesting independent evolutionary origins.
    • Sequence alignment identified significant differences in the active site of B compared to trypsin and chymotrypsin.

    Conclusions:

    • The unique structural elements in the Bb fragment likely contribute to its function as a cofactor-binding domain for C3b.
    • The identified sequence homologies in Ba suggest a distinct evolutionary path for the complement factor B gene.
    • The 'altered' regions in the active site of B may play a role in the formation of the C3 convertase catalytic site.