Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Domains in human plasminogen.

V V Novokhatny, S A Kudinov, P L Privalov

    Journal of Molecular Biology
    |October 25, 1984
    PubMed
    Summary

    Human plasminogen is composed of seven structural domains, including five kringle domains. Specific kringle domains bind lysine, and domain interactions change upon activation to plasmin.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    Thermodynamic basis of the α-helix and DNA duplex.

    European biophysics journal : EBJ·2021
    Same author

    Heat denaturation of ribonuclease.

    Biophysical chemistry·2012
    Same author

    Unfolding of bZIP dimers formed by the ATF-2 and c-Jun transcription factors is not a simple two-state transition.

    Biophysical chemistry·2010
    Same author

    Stability and DNA-binding ability of the bZIP dimers formed by the ATF-2 and c-Jun transcription factors.

    Journal of molecular biology·2009
    Same author

    [Role of carboxypeptidase in regulation of fibrinolysis].

    Ukrains'kyi biokhimichnyi zhurnal (1999 )·2009
    Same author

    Assembling the human IFN-beta enhanceosome in solution.

    Journal of molecular biology·2008

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Protein Structure

    Background:

    • Human plasminogen is a key protein in the fibrinolytic system.
    • Understanding its domain structure is crucial for comprehending its activation and function.

    Purpose of the Study:

    • To investigate the domain organization and stability of human plasminogen using calorimetric methods.
    • To identify lysine-binding sites within plasminogen domains.
    • To elucidate the structural changes occurring during plasminogen activation to plasmin.

    Main Methods:

    • Calorimetric studies of intramolecular melting.
    • Analysis of human plasminogen and its fragments under varied solvent conditions.
    • Investigation of the effect of epsilon-aminocaproic acid on domain stability.

    Main Results:

    • Intact plasminogen comprises seven compact, co-operative structural domains.
    • Five domains correspond to kringles, and two form the light chain of plasmin.
    • Epsilon-aminocaproic acid stabilizes kringle domains 1, 4, and 2, indicating lysine-binding ability.
    • Domain interactions change upon activation to plasmin, affecting the stability of the light chain domains.

    Conclusions:

    • Plasminogen's structure is modular, with distinct domains contributing to its function.
    • Lysine-binding is localized to specific kringle domains.
    • Activation to plasmin involves significant domain decooperation, particularly affecting the light chain and active site structure.

    Related Experiment Videos