Understanding the complementarity and plasticity of antibody-antigen interfaces.

ABSTRACT:

Motivation

While antibodies have been ground-breaking therapeutic agents, the structural determinants for antibody binding specificity remain to be fully elucidated, which is compounded by the virtually unlimited repertoire of antigens they can recognize. Here, we have explored the structural landscapes of antibody-antigen interfaces to identify the structural determinants driving target recognition by assessing concavity and interatomic interactions.

Results

We found that complementarity-determining regions utilized deeper concavity with their longer H3 loops, especially H3 loops of nanobody showing the deepest use of concavity. Of all amino acid residues found in complementarity-determining regions, tryptophan used deeper concavity, especially in nanobodies, making it suit

SUBMITTER: Myung Y 

PROVIDER: S-EPMC10329492 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature