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Related Experiment Videos

Third component of human complement: localization of the internal thiolester bond.

M L Thomas, J Janatova, W R Gray

    Proceedings of the National Academy of Sciences of the United States of America
    |February 1, 1982
    PubMed
    Summary

    Human complement protein C3

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    Area of Science:

    • Biochemistry
    • Immunology
    • Protein Chemistry

    Background:

    • Human complement protein C3 is a key component of the immune system.
    • Understanding its structure and function is crucial for immunology research.
    • The thiol ester group in C3 plays a significant role in its activation mechanism.

    Purpose of the Study:

    • To elucidate the precise location and structure of the C3d fragment within the alpha-chain of human complement protein C3.
    • To characterize the thiol ester site and its proximity to the amino terminus of C3d.
    • To investigate the structural relationships between C3, alpha(2)-macroglobulin, and C4.

    Main Methods:

    • Inactivation of human complement protein C3 using methylamine to generate a reactive SH group.
    • Coupling of C3 to activated thiol-Sepharose via the SH group, followed by elastase digestion.
    • Elution of the C3d fragment using L-cysteine and subsequent radiolabeling with iodo[2-(3H]acetic acid.
    • Partial sequence analysis of the radiolabeled C3d fragment and specific chemical cleavage of the alpha-chain after S-cyanylation.

    Main Results:

    • The thiol ester components of C3 are located near the amino terminus of the C3d fragment (residues 23 and 26).
    • Fragment C3d spans approximately positions 345-610 of the C3 alpha-chain.
    • Sequence comparison revealed identities between C3d and alpha(2)-macroglobulin around the thiol ester site and a glycosylation site.

    Conclusions:

    • The study provides a detailed structural map of the C3d fragment within the C3 alpha-chain.
    • The findings offer insights into the local folding constraints imposed by the thiol ester group and its role in C3 activation.
    • Identified sequence similarities suggest evolutionary or functional relationships among complement proteins and alpha(2)-macroglobulin.

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