Antibody structure
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Understanding Antibody Structure
Basic Structure of Antibodies
Antibodies, also known as immunoglobulins, are essential proteins of the immune system that recognize and neutralize foreign substances like viruses and bacteria. The fundamental structure of an antibody consists of two heavy chains and two light chains, forming a Y-shaped molecule 6. This configuration is consistent across all vertebrates, highlighting a common evolutionary origin 6.
Classes and Subclasses of Antibodies
Antibodies are categorized into different classes and subclasses based on their chemical and biological properties. These classes include IgG, IgA, IgM, IgE, and IgD, each with unique roles in the immune response 2. The diversity of antibodies is further enhanced by genetic recombination and mutation, allowing the immune system to produce a vast array of antibodies, each with a unique antigen-binding specificity 2.
Hypervariable Regions and Antigen Binding
The antigen-binding site of an antibody is located in the variable regions of the heavy and light chains, specifically within the complementarity-determining regions (CDRs). Among these, the H3 loop is particularly significant due to its high variability and crucial role in antigen binding 3. Accurate prediction of the H3 loop structure remains a challenge, but advancements in computational methods are making progress in this area 34.
Advances in Structural Prediction
Recent developments in artificial intelligence, such as AlphaFold2 and IgFold, have revolutionized the field of protein structure prediction. These tools leverage deep learning and massive datasets to predict antibody structures with high accuracy and speed 45. IgFold, for instance, uses a pre-trained language model on 558 million natural antibody sequences to predict structures in under a minute, significantly expanding the observed antibody structural space 5.
Functional Implications of Antibody Structure
The structure of antibodies is not only crucial for their antigen-binding capabilities but also for their interaction with other components of the immune system. Specific effector sites on antibodies interact with the complement system or cell surfaces to mediate immune responses such as lysis, opsonization, and hypersensitivity reactions 2. These interactions are essential for the biological expression of immune reactivity.
Engineering Therapeutic Antibodies
Understanding the structure-function relationship of antibodies has paved the way for the development of therapeutic antibodies. Protein engineering techniques have been employed to enhance antigen affinity, effector functions, and biophysical properties of antibodies, leading to the creation of various biologics for therapeutic use 8. These include antibody fragments, bispecific antibodies, and antibody fusion products, which are designed for improved efficacy and manufacturability 8.
Conclusion
The study of antibody structure has provided profound insights into their function and potential therapeutic applications. Advances in structural biology and computational prediction are continually enhancing our understanding and capabilities in antibody engineering, promising new avenues for medical treatments and immunological research.
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Most relevant research papers on this topic
Antibody Structure
Antiviral Fabs with novel structural features can effectively and broadly neutralize their targets, offering a promising approach for developing effective vaccines.
Antibody structure.
Antibodies have a unique basic structure, but their molecular modifications create a large variety of immunoglobulin classes and distinct combining specificities, affecting immune reactions.
Antibody H3 Structure Prediction
Computerized H3 structure prediction is crucial for accurate antibody binding site modeling and drug development, aiding rational design procedures.
Rigorous JournalFast, accurate antibody structure prediction from deep learning on massive set of natural antibodies
IgFold, a fast deep learning method, accurately predicts antibody structures in under one minute, expanding the observed structural space by over 40 fold.
Highly CitedStructure of Antibody Molecules
Antibody molecules, or immunoglobulins, have a similar structure consisting of two heavy and two light peptide chains, with recent studies focusing on the amino-acid sequences of these chains to understand antibody specificity, evolution, and genetic control of antibody synthesis.
ANTIBODY STRUCTURE AND MOLECULAR IMMUNOLOGY *
Molecular immunology has revolutionized immunological thought by linking antibody structure to antigen specificity and enabling experiments to test our arguments.
Highly CitedAntibody Structure and Function: The Basis for Engineering Therapeutics
Understanding antibody structure and function allows for engineering effective therapeutics with appropriate antigen affinity, effector function, and biophysical properties for various therapeutic applications.
Highly CitedThree-dimensional structure of an antibody-antigen complex.
The antilysozyme Fab-lysozyme complex reveals a complex interaction between the two proteins, with no water molecules found in the interface and a positive charge on Arg-45 and Arg-68 complementing the negative charge of Glu-35 and Glu-50 from the heavy chain.
Highly CitedAntibody-antigen interactions: new structures and new conformational changes.
New antibody structures reveal new insights into antibody-antigen interactions, enhancing our understanding of immunologically important molecules.
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