Structural trends in antibody-antigen binding interfaces: a computational analysis of 1833 experimentally determined 3D structures.

ABSTRACT: Antibodies are attractive therapeutic candidates due to their ability to bind cognate antigens with high affinity and specificity. Still, the underlying molecular rules governing the antibody-antigen interface remain poorly understood, making in silico antibody design inherently difficult and keeping the discovery and design of novel antibodies a costly and laborious process. This study investigates the characteristics of antibody-antigen binding interfaces through a computational analysis of more than 850,000 atom-atom contacts from the largest reported set of antibody-antigen complexes with 1833 nonredundant, experimentally determined structures. The analysis compares binding characteristics of conventional antibodies and single-domain antibodies (sdAbs) targeting both protein- and pepti

SUBMITTER: Madsen AV 

PROVIDER: S-EPMC10755492 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature