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Structure of Antibodies and Immunoglobulin Domains – Humoral Immunity

by Peter Delves, PhD
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    Let us look at the structure of an antibody molecule. They consist of two identical heavy chains, each of which is about 50 kilo Daltons in size. And two identical light chains, each of which is around about 25 kilo Daltons in size. So adding those together, we can see that the basic antibody molecule is around about 150 kilo Daltons. They vary a little bit from class to class, but that basic structure is around about 150 kilo Daltons. The two heavy chains are linked to each other by a disulfide bond. And each light chain is disulfide bonded to one of the heavy chains. This creates a very stable structure. Remember disulfide bonds are covalent bonds that are essentially irreversible. The antibody can be divided into two different parts - the Variable region and the Constant region. So here we can see the Variable region highlighted. And this is the part that varies from one antibody to another as the name suggests, and of course that’s related to the specificity of the antibody. In other words, to antigen binding. In contrast, the Constant regions of the antibody, particularly of the heavy chain are involved in the effector function of the antibody. That means what the antibody is actually going to go on and do in order to get rid of the particular infection. We can also divide the antibody up into what are called the Fab fragments - the Fragment antigen binding. Here, one of the Fragment antigen binding areas is indicated. And there are a total of two Fabs. And a Fragment crystallizable or Fc fragment which comprises the majority of the Constant region of the heavy chains. So here you can see the two Fabs and the Fc that comprise an antibody molecule. The light chain...

    About the Lecture

    The lecture Structure of Antibodies and Immunoglobulin Domains – Humoral Immunity by Peter Delves, PhD is from the course Humoral Immunity and Cell-Mediated Immunity. It contains the following chapters:

    • The Structure of Antibodies
    • Immunoglobulin Domains
    • Immunoglobulin Domains

    Included Quiz Questions

    1. IgA
    2. IgM
    3. IgG
    4. IgD
    5. IgE
    1. Light chains are attached to heavy chains with H+ bonds
    2. Made of two Fab regions and one Fc region
    3. Heavy chains are held together by disulfide bonds
    4. Approximate size is 150kDa
    5. Has a variable region and a constant region
    1. Kappa
    2. Mu
    3. Delta
    4. Gamma
    5. Epsilon
    1. IgM heavy chains- 4 constant region domains
    2. Light chains- 2 constant region domains
    3. IgA heavy chains- 2 constant region domains
    4. IgE heavy chains- 3 constant region domains
    5. IgD heavy chains- 4 constant region domains
    1. Are present on the constant region of both light and heavy chains
    2. Hypervariability
    3. Have amino acids that compliment the amino acid sequences in the antigen
    4. Six CDRs are present in each antigen binding site
    5. Three subdivisions of CDRs: CDR1, CDR2, and CDR3

    Author of lecture Structure of Antibodies and Immunoglobulin Domains – Humoral Immunity

     Peter Delves, PhD

    Peter Delves, PhD


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    Simply put
    By Hugh W. on 02. February 2017 for Structure of Antibodies and Immunoglobulin Domains – Humoral Immunity

    complete plain english, easy to understand and straight to the point