Abstract
Colorectal cancer (CRC) causes the second highest cancer-related deaths worldwide. The human A33 antigen is a validated immunotherapy target, which is homogeneously expressed in 95% cases of primary and metastatic colorectal cancers. In this article, we report the structure of a humanised antigen-binding fragment A33 (A33 Fab), a therapeutic antibody candidate, in two different crystal forms. Insights into the structural features of A33 Fab are provided with a focus on the grafted complementarity-determining regions (CDRs) and the switch linker between the variable and the constant regions.
Competing Interest Statement
The authors have declared no competing interest.
Copyright
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