Paratope
Paratope
The Paratope also known as the antigen-binding site, is the part of an antibody that makes contact with and recognizes an antigen. It is a small region of the antibody, typically made up of 15-22 amino acids, that is complementary in shape to a specific region on the antigen known as the epitope.
Structure[edit | edit source]
The paratope is located at the end of the antibody's Fab region. It is formed by the variable regions of the heavy and light chains of the antibody. These variable regions are unique to each antibody and are responsible for the antibody's specificity for its matching antigen.
Function[edit | edit source]
The paratope binds to the epitope on the antigen, forming an antigen-antibody complex. This binding is typically non-covalent and reversible, and is driven by a combination of hydrophobic interactions, hydrogen bonds, van der Waals forces, and ionic bonds. The strength of the binding, known as the affinity, is determined by the sum of these interactions.
Clinical significance[edit | edit source]
Understanding the structure and function of the paratope is important in the development of monoclonal antibodies for use in immunotherapy. By engineering antibodies with specific paratopes, it is possible to target specific antigens on the surface of cancer cells, for example, leading to their destruction by the immune system.
See also[edit | edit source]
References[edit | edit source]
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Contributors: Prab R. Tumpati, MD