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A model for fibrinogen: domains and sequence.

J W Weisel, C V Stauffacher, E Bullitt

    Science (New York, N.Y.)
    |December 20, 1985
    PubMed
    Summary
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    Researchers developed a low-resolution 3D model of fibrinogen, revealing how its protein chains fold into distinct globular domains. This structural insight aids understanding of fibrinogen

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Molecular Biology

    Background:

    • Fibrinogen is a key protein in blood coagulation.
    • Understanding fibrinogen's structure is crucial for elucidating its function.
    • Previous models lacked detailed domain information.

    Purpose of the Study:

    • To determine the three-dimensional structure of fibrinogen at low resolution.
    • To map the folding of the carboxyl-terminal regions of fibrinogen chains.
    • To develop a structural model based on experimental evidence.

    Main Methods:

    • Rotary-shadowed electron microscopy of modified fibrinogen.
    • Limited proteolysis using a bacterial protease for crystallization.
    • Image processing and X-ray analysis of fibrinogen crystals and fibrin.

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    Main Results:

    • Modified fibrinogen retained native structural features.
    • A three-dimensional low-resolution model of fibrinogen was developed.
    • The model identified distinct globular domains formed by carboxyl-termini of A alpha, B beta, and gamma chains.

    Conclusions:

    • Fibrinogen's carboxyl-terminal regions fold into independent globular domains.
    • The A alpha chain's carboxyl-terminus forms a central domain.
    • The B beta and gamma chain carboxyl-termini form proximal and distal end domains, respectively.