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  2. Immunoglobulin G - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_G

    The water-accessible surface area of an IgG antibody. Immunoglobulin G (IgG) is a type of antibody. Representing approximately 75% of serum antibodies in humans, IgG is the most common type of antibody found in blood circulation. [1] IgG molecules are created and released by plasma B cells. Each IgG antibody has two paratopes.

  3. Organization and expression of immunoglobulin genes

    en.wikipedia.org/wiki/Organization_and...

    When the B cells get activated, class switching can occur. The class switching involves switch regions that made up of multiple copies of short repeats (GAGCT and TGGGG). These switches occur at the level of rearrangements of the DNA because there is a looping event that chops off the constant regions for IgM and IgD and form the IgG mRNAs. Any ...

  4. Immunoglobulin class switching - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_class_switching

    Mechanism of class-switch recombination that allows isotype switching in activated B cells. Immunoglobulin class switching, also known as isotype switching, isotypic commutation or class-switch recombination (CSR), is a biological mechanism that changes a B cell's production of immunoglobulin from one type to another, such as from the isotype IgM to the isotype IgG. [1]

  5. Isotype (immunology) - Wikipedia

    en.wikipedia.org/wiki/Isotype_(immunology)

    IgG3 is an efficient activator of pro-inflammatory responses by triggering the classical complement pathway. [10] It has the shortest half-life compared to the other IgG subclasses [11] and is frequently present together with IgG1 in response to protein antigens after viral infections. [12]

  6. Immunoglobulin domain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_domain

    The immunoglobulin domain, also known as the immunoglobulin fold, is a type of protein domain that consists of a 2-layer sandwich of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek key topology, [1] [2] consisting of about 125 amino acids. The backbone switches repeatedly between the two β-sheets.

  7. Immunoglobulin heavy chain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_heavy_chain

    Each heavy chain has two regions: a constant region (which is the same for all immunoglobulins of the same class but differs between classes).. Heavy chains γ, α and δ have a constant region composed of three tandem (in a line next to each other) immunoglobulin domains but also have a hinge region for added flexibility.

  8. V (D)J recombination - Wikipedia

    en.wikipedia.org/wiki/V(D)J_recombination

    The process of V(D)J recombination is mediated by VDJ recombinase, which is a diverse collection of enzymes. The key enzymes involved are recombination activating genes 1 and 2 (RAG), terminal deoxynucleotidyl transferase (TdT), and Artemis nuclease, a member of the ubiquitous non-homologous end joining (NHEJ) pathway for DNA repair. [4]

  9. Complementarity-determining region - Wikipedia

    en.wikipedia.org/wiki/Complementarity...

    The "upper" part of an antibody.The complementarity-determining regions of the heavy chain are shown in red (. Complementarity-determining regions (CDRs) are polypeptide segments of the variable chains in immunoglobulins (antibodies) and T cell receptors, generated by B-cells and T-cells respectively.