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An antibody molecule. The two heavy chains are colored red, blue, and purple. The two light chains green and yellow. See also: The immunoglobulin light chain is the small polypeptide subunit of an antibody (immunoglobulin). A typical antibody is composed of two immunoglobulin (Ig) heavy chains and two Ig light chains.
The universal structure of antibody includes the constant regions part of the fragment crystallizable(Fc) region of the antibody (shown in dark blue). It also includes the fragment antigen binding which is composed of one heavy and one light chain (shown as L for light and H for heavy).
Rosetta Antibody is a novel antibody F V region structure prediction server, which incorporates sophisticated techniques to minimize CDR loops and optimize the relative orientation of the light and heavy chains, as well as homology models that predict successful docking of antibodies with their unique antigen. [138]
The structure of immunoglobulin polypeptide chain is dictated and controlled by number of genes encoded in the germ line. [2] However, these genes, as it was discovered by serologic and chemical methods, could be highly polymorphic. This polymorphism is subsequently projected to the overall amino acid structure of antibody chains.
Structure of a Fab with light and heavy chains. The fragment antigen-binding region (Fab region) is a region on an antibody that binds to antigens.It is composed of one constant and one variable domain of each of the heavy and the light chain.
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.
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.
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.