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. 2024 Mar 16;23:56. doi: 10.1186/s12943-024-01952-w

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 6 — Binding mode of G9 and G250 with CAIX. Depicts TAA, CAIX, gray, along with its transmembrane domain, intracellular tail and proteoglycan (PG) domain at the N-terminus. The variable regions of mAb, G9, are shown in pink bound to the predicted epitope and the variable regions of mAb G250, are shown in green. The zoomed view depicts the binding interface of G250 to CAIX (left) and G9 to CAIX (right, turned 90 degree) with epitopes colored in green and contact regions of the complementarity determining regions (CDRs) shown in yellow (heavy chain), and blue (light chains). G9 shows 2:1 binding mode to a CAIX dimer and G250 binds to a CAIX dimer in 1:1 ratio