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

2 -Microglobulin--a free immunoglobulin domain.

P A Peterson, B A Cunningham, I Berggård

    Proceedings of the National Academy of Sciences of the United States of America
    |July 1, 1972
    PubMed
    Summary

    Beta(2)-microglobulin shares sequence homology with immunoglobulin constant regions, particularly the C(H)3 domain. This suggests it functions as a free immunoglobulin domain, potentially similar to the C(H)3 domain of gamma1 heavy chains.

    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

    Regulation of internodal lenght by peroxidase enzymes in grain sorghum.

    TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·2014
    Same author

    Solution structure of the third immunoglobulin domain of the neural cell adhesion molecule N-CAM: can solution studies define the mechanism of homophilic binding?

    Journal of molecular biology·2001
    Same author

    A short segment within the cytoplasmic domain of the neural cell adhesion molecule (N-CAM) is essential for N-CAM-induced NF-kappa B activity in astrocytes.

    Proceedings of the National Academy of Sciences of the United States of America·2001
    Same author

    Benzocaine-associated methemoglobinemia following bronchoscopy in a healthy research participant.

    Respiratory care·2000
    Same author

    N-CAM binding inhibits the proliferation of hippocampal progenitor cells and promotes their differentiation to a neuronal phenotype.

    The Journal of neuroscience : the official journal of the Society for Neuroscience·2000
    Same author

    Schizophrenia and the mechanisms of conscious integration.

    Brain research. Brain research reviews·2000

    Area of Science:

    • Immunology
    • Structural Biology
    • Biochemistry

    Background:

    • Beta(2)-microglobulin is a protein found on the surface of most nucleated cells.
    • Its structural and functional relationship to immunoglobulins has been a subject of investigation.

    Purpose of the Study:

    • To analyze the primary structure of beta(2)-microglobulin.
    • To compare its sequence and structural features with known immunoglobulin domains.
    • To elucidate the potential functional role of beta(2)-microglobulin based on its structural similarities.

    Main Methods:

    • Primary sequence analysis of beta(2)-microglobulin.
    • Homology comparison with constant regions of immunoglobulin light chains (C(L)) and gamma1 heavy chains (C(H)1, C(H)2, C(H)3).
    • Analysis of intrachain disulfide loop size and comparison with immunoglobulin disulfide loops.

    Related Experiment Videos

    Main Results:

    • Beta(2)-microglobulin exhibits significant sequence homology to the constant portion of immunoglobulin light chains and the C(H)1, C(H)2, and C(H)3 regions of immunoglobulin G gamma1 heavy chains.
    • The homology is particularly pronounced with the C(H)3 region.
    • A 57-amino-acid intrachain disulfide loop was identified, comparable in size to those in immunoglobulin constant regions.
    • No significant homology was found with immunoglobulin variable regions.

    Conclusions:

    • Beta(2)-microglobulin is structurally analogous to a free immunoglobulin domain.
    • Its structural features suggest a potential effector function, possibly mirroring that of the C(H)3 domain of gamma1 immunoglobulin G heavy chains.