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IgG antibodies are large globular proteins made of four peptide chains; [6] two identical γ (gamma) heavy chains of about 50 kDa and two identical light chains of about 25 kDa. The resulting tetrameric quaternary structure, therefore, has a total molecular weight of about 150 kDa. [7]
In IgG, IgA and IgD antibody isotypes, the Fc region is composed of two identical protein fragments, derived from the second and third constant domains of the antibody's two heavy chains; IgM and IgE Fc regions contain three heavy chain constant domains (C H domains 2–4) in each polypeptide chain.
IgG is the most abundant antibody class in the serum and it is divided into 4 subclasses based on differences in the structure of the constant region genes and the ability to trigger different effector functions.
Free immunoglobulin light chains secreted by neoplastic plasma cells, such as in multiple myeloma, can be called Bence Jones protein when detected in the urine, although there is a trend to refer to these as urinary free light chains. Increased levels of free Ig light chains have also been detected in various inflammatory diseases.
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.
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.
The general structure of the B cell receptor includes a membrane-bound immunoglobulin molecule and a signal transduction region. Disulfide bridges connect the immunoglobulin isotype and the signal transduction region. The B-cell receptor is composed of two parts: A membrane-bound immunoglobulin molecule of one isotype (IgD, IgM, IgA, IgG, or IgE).
A single-domain antibody is a peptide chain of about 110 amino acids long, comprising one variable domain (V H) of a heavy-chain antibody, or of a common IgG.These peptides have similar affinity to antigens as whole antibodies, but are more heat-resistant and stable towards detergents and high concentrations of urea.
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