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Antibody Structure
Robyn L Stanfield1, Ian A Wilson1
1Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037.
Microbiology Spectrum
|June 25, 2015
Abstract:
A brief outline of antibody structure is followed by highlights from several recently determined crystal structures of human, antiviral Fabs. These Fabs all have novel structural features that allow them to potently and broadly neutralize their targets.
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Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
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Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
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