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. 2019 Jul 19;10:3192. doi: 10.1038/s41467-019-11173-1

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© The Author(s) 2019

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — Comparison of Bcl-xL/HBx-aa113–135, Bcl-xL/ABT-263, Bcl-xL/ABT-737, and Bcl-2/HBx-aa110–135 structures. a Cartoon structure of Bcl-xL in complex with HBx-aa113–135 (PDB ID 5B1Z). b Cartoon structure of Bcl-xL in complex with ABT-263 (PDB ID 4QNQ). c Cartoon structure of Bcl-2 in complex with ABT-737 (PDB ID 2YXJ²³). d Cartoon structure of Bcl-2 in complex with HBx-aa110–135 (PDB ID 5FCG⁸). The structures of Bcl-xL and Bcl-2 are in surface mode, the HBx-BH3-like motifs are in cartoon mode, and key residues and ABT molecules are indicated in stick mode. Notably, compared with the Bcl-xL/HBx-aa113–135 structure, the HBx-BH3-like helix in the Bcl-2/HBx-aa110–135 structure is shifted ~8 Å towards the N-terminus. Hence, the side chain of the crucial Trp120 residue is pointing to the opposite direction and more than 10 Å away from the conserved hydrophobic pocket formed by the side chains of Phe105, Leu108, Val126, and Phe146 that is critical for binding the HBx-BH3-like motif. e, f The structural superimposition (front and side views) of Bcl-xL/HBx-BH3-like complex, Bcl-xL/ABT-263 complex, Bcl-xL/ABT-737 complex, and Bcl-2/HBx-BH3-like complex. Bcl-xL and Bcl-2 are colored in dark gray. The HBx-BH3-like peptide in the Bcl-xL/HBx-BH3-like complex, ABT-263, ABT-737, and the HBx-BH3-like peptide in the Bcl-2/HBx-BH3-like complex are colored in green, red, blue, and cyan, respectively