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Related Experiment Videos

Structure of human factor VIII.

G A Vehar, B Keyt, D Eaton

    Nature
    |November 22, 1984
    PubMed
    Summary
    This summary is machine-generated.

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    Human factor VIII, a protein crucial for blood clotting, has a unique domain structure. Its DNA sequence reveals similarities to ceruloplasmin, aiding in understanding its activation and inactivation.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Genetics

    Background:

    • Human factor VIII (FVIII) is essential for hemostasis.
    • Understanding FVIII's structure and function is critical for treating bleeding disorders.

    Purpose of the Study:

    • To deduce the amino acid sequence of human factor VIII from its DNA sequence.
    • To identify structural domains and homologies of factor VIII.
    • To predict domains involved in factor VIII activation and inactivation.

    Main Methods:

    • DNA sequencing to deduce the amino acid sequence of human factor VIII.
    • Sequence homology analysis comparing factor VIII to other proteins.
    • Identification of thrombin cleavage sites in plasma-derived factor VIII.

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    Main Results:

    • The mature human factor VIII polypeptide consists of 2,332 amino acids.
    • Factor VIII exhibits a triplicated domain structure.
    • A 35% sequence homology was found between factor VIII and ceruloplasmin.
    • Thrombin cleavage sites were mapped, allowing prediction of functionally relevant domains.

    Conclusions:

    • The deduced sequence and domain structure provide insights into factor VIII's molecular organization.
    • Homology with ceruloplasmin suggests potential shared functional or evolutionary aspects.
    • Mapping cleavage sites aids in understanding the mechanisms of factor VIII activation and inactivation.