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Related Experiment Videos

Structure of thrombospondin.

J E Coligan, H S Slayter

    The Journal of Biological Chemistry
    |March 25, 1984
    PubMed
    Summary
    This summary is machine-generated.

    Thrombospondin

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Structural Biology

    Background:

    • Thrombospondin is a multifunctional protein involved in various cellular processes.
    • Understanding its structure is crucial for elucidating its biological functions.

    Purpose of the Study:

    • To characterize the structural and functional domains of thrombospondin.
    • To identify the location of the heparin-binding site within the thrombospondin molecule.

    Main Methods:

    • NH2-terminal amino acid sequencing
    • Plasmin digestion and peptide analysis
    • Electron microscopy of tungsten-shadowed replicas

    Main Results:

    • Identical NH2-terminal sequences for thrombospondin and its 30-kDa heparin-binding peptide.

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  • Electron microscopy revealed a tripartite 'bola-like' structure (~60 nm).
  • Heparin-binding peptide and a 20-kDa peptide are located in the globular head regions, which are removed by plasmin digestion.

    • Conclusions:

    • The heparin-binding domain of thrombospondin is located in its NH2-terminal head region.
    • Thrombospondin possesses a unique bola-like quaternary structure with distinct head and leg domains.
    • Proteolytic cleavage by plasmin releases key functional peptides from the head regions.