Antibody-protein binding and conformational changes: identifying allosteric signalling pathways to engineer a better effector response.

ABSTRACT: Numerous monoclonal antibodies have been developed successfully for the treatment of various diseases. Nevertheless, the development of biotherapeutic antibodies is complex, expensive, and time-consuming, and to facilitate this process, careful structural analysis beyond the antibody binding site is required to develop a more efficacious antibody. In this work, we focused on protein antigens, since they induce the largest antibody changes, and provide interesting cases to compare and contrast. The structures of 15 anti-protein antibodies were analysed to compare the antigen-bound/unbound forms. Surprisingly, three different classes of binding-induced changes were identified. In class (B1), the antigen binding fragment distorted significantly, and we found changes in the loop region of the

SUBMITTER: Al Qaraghuli MM 

PROVIDER: S-EPMC7426963 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature