Antibody structure, prediction and redesign
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Updated: Oct 30, 2026

Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy
Published on: August 15, 2014
V Morea1, A Tramontano, M Rustici
1IRBM P. Angeletti, Pomezia, Italy.
So far the difficulty to predict the structure of the third hypervariable loop of the heavy chain of antibodies has represented the main limitation in modelling the complete antigen binding site. We carefully analysed all available structures of immunoglobulins searching for rules relating the loop conformation to its amino acid sequence. Here, we analyse the conformation of this loop and show that we are able to predict the conformation of the ten residues proximal to the framework. The conformation of the remaining residues of loops longer than 10 residues can also be predicted in many cases. This, combined with the previously defined canonical structures for the other five hypervariable loops, is an important step toward the prediction of the complete immunoglobulin antigen-binding site. We exemplify our prediction protocol using three known immunoglobulin structures as test cases.
So far the difficulty to predict the structure of the third hypervariable loop of the heavy chain of antibodies has represented the main limitation in modelling the complete antigen binding site. We carefully analysed all available structures of immunoglobulins searching for rules relating the loop conformation to its amino acid sequence. Here, we analyse the conformation of this loop and show that we are able to predict the conformation of the ten residues proximal to the framework. The conformation of the remaining residues of loops longer than 10 residues can also be predicted in many cases. This, combined with the previously defined canonical structures for the other five hypervariable loops, is an important step toward the prediction of the complete immunoglobulin antigen-binding site. We exemplify our prediction protocol using three known immunoglobulin structures as test cases.
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Antibody Structure
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.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibody Structure
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.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibody Structure and Classes
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.
Antibody Actions
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
Cross-reactivity
Protein Organization
The primary structure of a protein is its amino acid sequence.
