Mobility and Disorder in Antibody and Antigen Binding Sites Do Not Prevent Immunochemical Recognition
Document Type
Article
Publication Date
2021
Keywords
Antibody, antigen, intrinsic disorder, immunochemical recognition, polyspecificity
Digital Object Identifier (DOI)
https://doi.org/10.1080/10409238.2020.1869683
Abstract
The known polyspecificity of antibodies, which is crucial for efficient immune response, is determined by the conformational flexibility and intrinsic disorder encoded in local peculiarities of the amino acid sequence of antibodies within or in the vicinity of their complementarity determining regions. Similarly, epitopes represent fuzzy binding sites, which are also characterized by local structural flexibility. Existing data suggest that the efficient interactions between antigens and antibodies rely on the conformational mobility and some disorder of their binding sites and therefore can be relatively well described by the “flexible lock – adjustable key” model, whereas both, extreme order (rigid lock-and-key) and extreme disorder (viral shape-shifters) are not compatible with the efficient antigen-antibody interactions and are not present in immune interactions.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Critical Reviews in Biochemistry and Molecular Biology, v. 56, issue 2, p. 149-156
Scholar Commons Citation
Uversky, Vladimir N. and Regenmortel, Marc H., "Mobility and Disorder in Antibody and Antigen Binding Sites Do Not Prevent Immunochemical Recognition" (2021). Molecular Medicine Faculty Publications. 199.
https://digitalcommons.usf.edu/mme_facpub/199
