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How Are Antibodies Structured?

Published in Immunology 3 mins read

Antibodies are Y-shaped proteins crucial to the immune system. Their structure is essential for their function in recognizing and neutralizing foreign substances (antigens).

Antibody Structure: A Detailed Look

The basic antibody unit comprises four polypeptide chains: two identical heavy chains (H chains) and two identical light chains (L chains). These chains are linked by disulfide bonds, creating the characteristic Y shape. Sino Biological describes this Y-shape clearly.

  • Light Chains: These come in two types: kappa (κ) and lambda (λ). Bio X Cell notes this classification. Each light chain contains approximately 220 amino acids.
  • Heavy Chains: These chains determine the antibody's isotype (IgA, IgD, IgE, IgG, or IgM), influencing its function and location within the body. Wikipedia details these five classes. Each heavy chain is longer than a light chain.
  • Variable Regions (Fab): The "arms" of the Y shape comprise the variable regions (Fab fragments). These regions possess unique amino acid sequences that bind specifically to particular antigens. This specific binding is a key component of antibody function.
  • Constant Region (Fc): The "stem" of the Y, known as the Fc region (fragment crystallizable), is relatively constant across different antibodies of the same isotype. This region interacts with immune system cells, triggering downstream responses like phagocytosis (engulfing and destroying pathogens) and complement activation (a cascade of immune reactions). Sino Biological explains the functions of the Fab and Fc regions.
  • Flexible Tether: The connection between the Fab and Fc regions allows flexibility in antigen binding, enabling antibodies to effectively interact with antigens in various conformations. This is mentioned as a key structural feature in the provided reference, stating antibodies are "loosely connected by a flexible tether."

Visualizing the Antibody Structure

Multiple sources, including research papers like those detailing COVID-19 antibody structures (Fred Hutch), utilize 3D imaging and X-ray crystallography to visualize the antibody structure. These techniques allow detailed analyses of the antibody-antigen interaction at the molecular level. The reference mentions schematic representations of antibody structure determined by X-ray crystallography.

Beyond the Basic Unit

While the basic four-chain structure is fundamental, it's important to note antibodies are glycoproteins; they also contain carbohydrate molecules attached to the protein backbone, further influencing their function and interaction with other molecules.

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