Image by freepik Antibodies rely on their complementarity-determining regions (CDRs) to recognize and bind antigens with high specificity. Among these regions, CDR3-particularly in the heavy chain (CDR-H3)-exhibits remarkable length diversity, directly influencing antigen recognition, structural stability, and therapeutic efficacy. Understanding how CDR length shapes antibody functionality is critical for advancing biologics, diagnostics, and immunotherapy . The Role of CDR-H3 in Antibody Diversity CDR-H3 is the most variable region in antibodies, formed by the recombination of V, D, and J gene segments. Its length ranges widely: Human antibodies: Typically, 11–20 amino acids (median 14), forming a near-normal distribution. Bovine antibodies: Feature ultra-long CDR-H3s (>50 residues) with unique "stalk-knob" structures for deep antigen binding. This length diversity expands the antibody repertoire, enabling recognition of structurally diverse antigens, from small molecul...
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