Interactions of protein antigens with antibodies
| Autor: | Gerson H. Cohen, David R. Davies |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1996 |
| Předmět: |
Models
Molecular Conformational change Stereochemistry Protein Conformation Neuraminidase Epitope Antigen-Antibody Reactions Epitopes Immunoglobulin Fab Fragments Mice Structure-Activity Relationship Protein structure Antigen Bacterial Proteins Orthomyxoviridae Infections X-Ray Diffraction Animals Binding site Phosphoenolpyruvate Sugar Phosphotransferase System Antigens Viral Multidisciplinary biology Chemistry Antibodies Monoclonal Molecular biology Antibodies Anti-Idiotypic Epitope mapping biology.protein Muramidase Binding Sites Antibody Antibody Chickens Epitope Mapping Research Article Protein Binding |
| Popis: | There are now several crystal structures of antibody Fab fragments complexed to their protein antigens. These include Fab complexes with lysozyme, two Fab complexes with influenza virus neuraminidase, and three Fab complexes with their anti-idiotype Fabs. The pattern of binding that emerges is similar to that found with other protein-protein interactions, with good shape complementarity between the interacting surfaces and reasonable juxtapositions of polar residues so as to permit hydrogen-bond formation. Water molecules have been observed in cavities within the interface and on the periphery, where they often form bridging hydrogen bonds between antibody and antigen. For the most part the antigen is bound in the middle of the antibody combining site with most of the six complementarity-determining residues involved in binding. For the most studied antigen, lysozyme, the epitopes for four antibodies occupy approximately 45% of the accessible surface area. Some conformational changes have been observed to accompany binding in both the antibody and the antigen, although most of the information on conformational change in the latter comes from studies of complexes with small antigens. |
| Databáze: | OpenAIRE |
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