Antibody CDR amino acids underlying the functionality of antibody repertoires in recognizing diverse protein antigens.

ABSTRACT: Antibodies recognize protein antigens with exquisite specificity in a complex aqueous environment, where interfacial waters are an integral part of the antibody-protein complex interfaces. In this work, we elucidate, with computational analyses, the principles governing the antibodies' specificity and affinity towards their cognate protein antigens in the presence of explicit interfacial waters. Experimentally, in four model antibody-protein complexes, we compared the contributions of the interaction types in antibody-protein antigen complex interfaces with the antibody variants selected from phage-displayed synthetic antibody libraries. Evidently, the specific interactions involving a subset of aromatic CDR (complementarity determining region) residues largely form the predominant determi

SUBMITTER: Peng HP 

PROVIDER: S-EPMC9307644 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature