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Related Experiment Videos

Fibronectin molecule visualized in electron microscopy: a long, thin, flexible strand

H P Erickson, N Carrell, J McDonagh

    The Journal of Cell Biology
    |December 1, 1981
    PubMed
    Summary

    Plasma fibronectin, a large dimeric protein, has a long, flexible strand structure. Electron microscopy reveals its molecular architecture, with polypeptide chains extending from the center to the ends.

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    Area of Science:

    • Biochemistry
    • Structural Biology
    • Molecular Biology

    Background:

    • Fibronectin is a crucial extracellular matrix protein involved in cell adhesion and tissue repair.
    • Understanding fibronectin's structure is essential for elucidating its biological functions.

    Purpose of the Study:

    • To determine the three-dimensional structure of plasma fibronectin.
    • To elucidate the molecular organization of the fibronectin dimer.

    Main Methods:

    • Electron microscopy of shadowed specimens.
    • Limited proteolysis with plasmin.
    • Analysis of fibronectin-fibrinogen complexes.

    Main Results:

    • Plasma fibronectin (440,000 MW) is a long, thin, flexible strand (160 nm extended length, 2 nm diameter).

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  • No large globular domains were observed; fragments from plasmin digestion are segments of the strand.
  • Fibronectin-fibrinogen complexes show fibrinogen attachment at the fibronectin strand ends.

    • Conclusions:

    • Each polypeptide chain of the fibronectin dimer spans half the strand length.
    • Carboxyl termini are joined at the center, and amino termini are at the ends.
    • This structural model explains fibronectin's interactions with other molecules.