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. 2024 Jan 7;14:742. doi: 10.1038/s41598-023-50262-6

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© The Author(s) 2023

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/.

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The lirilumab epitope overlaps with the HLA binding site but is not exposed on KIR3D class receptors. (Left) KIR2DL3 bound to Fab^Lirulumab, with the Fab^Lirulumab heavy chain colored navy, light chain colored light blue, KIR2DL3 domain 1 colored gold and domain 2 colored white. (Center) KIR2DL1 bound to HLA-Cw4 (PDB 1im9)³⁸, with HLA colored gray and KIR2DL1 colored bronze. (Right) KIR3DL1 bound to HLA-B*57:03 (PDB 6v3j)³⁹, with HLA colored gray and KIR3DL1 colored olive. Dashed lines represent the locations of transmembrane domains. There is an approximate 134 Å² overlap between the lirilumab epitope and the HLA binding site, revealing how lirilumab can block HLA binding. Also, these structures reveal that the lirilumab epitope is occluded by the additional domain of KIR3D receptors, explaining why lirilumab does not bind KIR3D receptors.