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. 2015 Jul 2;6(7):e1804. doi: 10.1038/cddis.2015.118

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Copyright © 2015 Macmillan Publishers Limited

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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Structural analysis of the interaction between BCL-X_L and p-BH3_BIM(R154S/I155R/E158S). (a) Crystal structure of the BCL-X_L−p-BH3_BIM(R154S/I155R/E158S) complex. BCL-X_L is shown as an electrostatic surface model with the bound peptide in green. The electrostatic potential is shown at the bottom. (b) Detailed interactions of the Arg155 of p-BH3_BIM(R154S/I155R/E158S) in the complex. Polar interactions are indicated by dotted lines with the distances noted. The aliphatic chain of Arg155 has a hydrophobic interaction with the Tyr101 of BCL-X_L. (c) Detailed phosphoserine-mediated intermolecular interactions