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. 2017 Jan 12;8(1):e2543. doi: 10.1038/cddis.2016.469

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Copyright © 2017 The Author(s)

Cell Death and Disease is an open-access journal published by Nature Publishing Group. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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(a) Detailed view of the BHP2:LB-Bak-2 BH3 interface. The BHP2 surface, backbone and binding groove are shown in gray and pink respectively, whereas LB-Bak-2 BH3 is shown in violet. The four key hydrophobic residues of LB-Bak-2 (V71, L75, F78 and V82) on protruding into the binding groove, and the conserved salt bridge formed by LB-Bak D80 and BHP2 R135 are labeled, as well as residues involved in hydrogen bonds. Comparison of the P3 pocket among pro-survival Bcl-2: pro-apoptotic BH3 domain complexes. (b) BHP2:LB-Bak-2 complex. (c) Bcl-x_L:Bim complex. (d) CED9:EGL1 complex. (e) F1L:Bak complex