Specific attributes of the V_L domain influence both the structure and structural variability of CDR-H3 through steric effects.

ABSTRACT: Antibodies, through their ability to target virtually any epitope, play a key role in driving the adaptive immune response in jawed vertebrates. The binding domains of standard antibodies are their variable light (V_L) and heavy (V_H) domains, both of which present analogous complementarity-determining region (CDR) loops. It has long been known that the V_H CDRs contribute more heavily to the antigen-binding surface (paratope), with the CDR-H3 loop providing a major modality for the generation of diverse paratopes. Here, we provide evidence for an additional role of the V_L domain as a modulator of CDR-H3 structure, using a diverse set of antibody crystal structures and a large set of molecular dynamics simulations. We show that specific attributes o

SUBMITTER: Guloglu B 

PROVIDER: S-EPMC10410447 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature