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  2. Organization and expression of immunoglobulin genes

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

    Antibody (or immunoglobulin) structure is made up of two heavy-chains and two light-chains. These chains are held together by disulfide bonds. The arrangement or processes that put together different parts of this antibody molecule play important role in antibody diversity and production of different subclasses or classes of antibodies.

  3. Immunoglobulin heavy chain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_heavy_chain

    These heavy chain types vary between different animals. All heavy chains contain a series of immunoglobulin domains, usually with one variable domain (V H) that is important for binding antigen and several constant domains (C H 1, C H 2, etc.). Production of a viable heavy chain is a key step in B cell maturation. If the heavy chain is able to ...

  4. File:Immunoglobulin basic unit.svg - Wikipedia

    en.wikipedia.org/wiki/File:Immunoglobulin_basic...

    English: Schematic diagram of the basic unit of immunoglobulin (antibody) Fab; Fc; heavy chain (consist of VH, CH1, hinge, CH2 and CH3 regions: from N-term) light chain (consist of VL and CL regions: from N-term) antigen binding site; hinge regions (*) -S-S-mean disulfide bonds.

  5. Immunoglobulin superfamily - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_superfamily

    In humans, there are five distinct types of immunoglobulin molecule all containing a heavy chain with four Ig domains and a light chain with two Ig domains. The antigen receptor of T cells is the T-cell receptor (TCR), which is composed of two chains, either the TCR-alpha and -beta chains, or the TCR-delta and gamma chains.

  6. Complementarity-determining region - Wikipedia

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

    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. CDRs are where these molecules bind to their specific antigen and their structure/sequence determines the binding activity of the respective antibody.

  7. Framework region - Wikipedia

    en.wikipedia.org/wiki/Framework_region

    The antibody has a three-dimensional structure with beta pleated sheet and alpha helices. [5] The antibody folds so the variable regions form three loops with the framework regions folded into one another and the CDR regions on the tips of each of these loops in direct contact with the antigen.

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  9. Immunoglobulin C2-set domain - Wikipedia

    en.wikipedia.org/wiki/Immunoglobulin_C2-set_domain

    There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha, delta, epsilon, gamma and mu, all consisting of a variable domain (VH) and three (in alpha, delta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4).