Molecular recognition in antibody-antigen complexes.

Eric J Sundberg; Roy A Mariuzza

doi:10.1016/s0065-3233(02)61004-6

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Molecular recognition in antibody-antigen complexes.

Eric J Sundberg·Roy A Mariuzza

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Abstract

With the numerous detailed molecular descriptions of antibody-antigen interfaces, the structual study of these molecular interactions has evolved from an attempt to understand to immunological function to their use as model systems for protein-protein interactions. In this chapter, we describe the structual aspects common to antibody-antigen interfaces and discuss the roles they may play in antibody cross-rectivity and molecular mimicry. More detailed analysis of these interfaces has required the marriage of structural studies with extensive mutagenesis and thermodynamic analysis efforts. Here, we discuss the thermodynamic mapping of interfaces for two model antibody-antigen complexes, including the identification of thermodynamic hot spots in binding and the various mechanism used to accommodate interface mutations. We also discuss the functional roles for protein plasticity in antigen recognition, including the entropic control of antibody affinity maturation and the use of induced fit mechanism of different types and to varying degrees by mature antibodies in binding their specific antigens.

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Animals Antigen-Antibody Complex Binding Sites, Antibody Cross Reactions Humans Models, Immunological Models, Molecular Molecular Mimicry Mutation Protein Binding Protein Conformation Proteins Thermodynamics Journal Article Review

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Eric J Sundberg, Roy A Mariuzza. 2002. Molecular recognition in antibody-antigen complexes.. https://doi.org/10.1016/s0065-3233(02)61004-6

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