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. 2011 Aug 12;438(Pt 2):291–301. doi: 10.1042/BJ20110257

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© 2011 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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(A) A dimer of human Bcl-xL (Δ27–82) showing swapping of the α1 domains. The two helical SOUL BH3 peptides are represented in red. (B) A protomer of Bcl-xL and the SOUL BH3 peptide in contact with it. The portion of the peptide predicted by sequence homology to be the BH3 domain is in blue, whereas the yellow part is the additional portion of the peptide, the beginning of the second helix of SOUL. (C) Electron density of the SOUL BH3 peptide bound to Bcl-xL oriented as in (B). The molecular surface of Bcl-xL shows the negatively charged residues in red and those positively charged in blue. The 2F_obs−F_c map was contoured at a 1.2 σ level. Selected BH3 peptide amino acids participating in important contacts with Bcl-xL have been labelled in single-letter amino acid notation. The Figure was prepared using the program PyMOL (http://www.pymol.org).