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. 2023 Jul 4;24:157. doi: 10.1186/s13059-023-02995-w

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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/. 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. 5 — The potential functional differentiation between KLRC2 and KLRC3 by natural selection in primate evolution. a The phylogenetic tree reconstructed from KLRC2 and KLRC3 of humans and other NHPs with BEAST2 shows the duplication of KLRC2 and KLRC3 occurred at the common ancestor of African great apes. The 95% confidence interval of the estimated age of each node is shown in the blue bar. All nodes are supported by one posterior possibility shown in dark circle dots. The texts: C, B, G, O, Mac, Mar, and Owl in the tips represent chimpanzee, bonobo, gorilla, orangutan, macaque, marmoset, and owl monkey, respectively. b The possibility of amino acid under positive selection inferred by the branch-site model in PAML is shown on the top panel. The gray, orange, and blue dots represent the possibility of less than 0.9, between 0.9 and 0.95, or greater than 0.95, respectively. The amino acid alignment of KLRC2 and KLRC3 among primates is shown on the bottom right panel. Structure alignment of predicted structures of KLRC2 from residue 118 to 231 (orange, Uniprot: P26717) and KLRC3 from residue 118 to 240 (cyan, Uniprot: Q07444). The zoomed-in pictures depict the structural discrepancies in the loop (top) and the following β-sheet (bottom) between KLRC2 and KLRC3. c Predicted structures of KLRC/HLA-E/CD94 complex (KLRC2 from residue 118 to 231: orange, Uniprot: P26717; KLRC3 from residue 118 to 240: cyan, Uniprot: Q07444; Full-length HLA-E: purple, Uniprot: I3RW89; CD94 from residue 57 to 179: green, Uniprot: Q13241). The zoomed-in protein structure depicts the interaction interfaces of KLRC2/HLA-E (top) and KLRC3/HLA-E (bottom)