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. 2012 Jun 14;8(6):e1002565. doi: 10.1371/journal.pcbi.1002565

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Ionescu et al.

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 author and source are properly credited.

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(A) Sequence alignment of central helices of Bak and Bax. An asterisk indicates a single, fully conserved residue. A colon indicates conservation between groups of strongly similar biochemical properties. A period indicates conservation between groups of weakly similar biochemical properties. The residues involved in the charge transfer network in Bax are conserved in Bak as Trp125, Arg127 and Arg137. (B) Bak structure (ochre) is displayed according to Figure 5B, with the same top view of the central helix, and the same color coding for C-domain (yellow), BH3-domain (cyan), central helix (green) and hub residues (red and blue). Residues Trp125, Arg127 and Arg137 are organized in a similar manner to their Bax homologues, suggesting that they may also play an essential role during Bak activation.