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The structure of the humanised A33 Fab C226S variant, an immunotherapy candidate for colorectal cancer

Jiazhi Tang, Cheng Zhang, Paul Dalby, Frank Kozielski
doi: https://doi.org/10.1101/2022.06.21.497004
Jiazhi Tang
1UCL School of Pharmacy, 29-39 Brunswick Square, London WC1N 1AX, UK
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Cheng Zhang
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Paul Dalby
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  • For correspondence: f.kozielski@ucl.ac.uk p.dalby@ucl.ac.uk
Frank Kozielski
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  • For correspondence: f.kozielski@ucl.ac.uk p.dalby@ucl.ac.uk
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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.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted June 21, 2022.
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The structure of the humanised A33 Fab C226S variant, an immunotherapy candidate for colorectal cancer
Jiazhi Tang, Cheng Zhang, Paul Dalby, Frank Kozielski
bioRxiv 2022.06.21.497004; doi: https://doi.org/10.1101/2022.06.21.497004
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The structure of the humanised A33 Fab C226S variant, an immunotherapy candidate for colorectal cancer
Jiazhi Tang, Cheng Zhang, Paul Dalby, Frank Kozielski
bioRxiv 2022.06.21.497004; doi: https://doi.org/10.1101/2022.06.21.497004

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