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. 2018 May 11;42(2):905–918. doi: 10.3892/ijmm.2018.3672

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Copyright: © Chu et al.

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

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Domain structure and sequence of the BH3-like motifs in Beclin-1 and BCL2L12. The helix structure of BCL2L12 and the BH3 domain of both Beclin-1 and BCL2L12 are shown. A 12-residue region is diagramed to represent the BH3 domain defined in the present study. The LXXXXD (for other BCL2 family proteins) or LXXXAE/D (for BCL2L12) motif is drawn and critical residues comprising L213 (h1, position −4 corresponding to LXXXAE/D motif), L217 (h2, position 0) and I224 (h4, position +7) that affect interaction between BCL2L12 and BCL2/BCL-XL are highlighted in yellow. BCL2L12, BCL2-like 12; BCL2, BCL2 apoptosis regulator; BCL-XL, BCL-extra large.