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Related Experiment Videos

Tumour necrosis factor is a compact trimer.

P Wingfield, R H Pain, S Craig

    FEBS Letters
    |January 26, 1987
    PubMed
    Summary
    This summary is machine-generated.

    Recombinant human tumor necrosis factor (TNF) forms a stable trimer. Unfolded TNF subunits can spontaneously refold and assemble into biologically active protein structures.

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    Area of Science:

    • Biochemistry
    • Structural Biology
    • Immunology

    Background:

    • Tumor necrosis factor (TNF) is a key inflammatory cytokine.
    • Understanding TNF's structure is crucial for therapeutic development.

    Purpose of the Study:

    • To characterize the subunit structure of recombinant human TNF.
    • To investigate the folding and assembly properties of TNF.

    Main Methods:

    • Studied recombinant human TNF.
    • Characterized protein subunit structure and quaternary association.
    • Assessed thermodynamic stability and refolding capabilities.

    Main Results:

    • Human TNF is a trimer (Mr 52000) with subunits in a compact, triangular arrangement.

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  • TNF belongs to the all-beta class of proteins.
  • Demonstrated high thermodynamic stability and spontaneous refolding/association of subunits into active TNF.

    • Conclusions:

    • Recombinant human TNF exhibits a stable trimeric structure.
    • TNF subunits possess intrinsic properties for spontaneous refolding and assembly into biologically active forms.