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. 2022 Jun 28;3(3):375–391. doi: 10.37349/etat.2022.00088

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© The Author(s) 2022.

This is an Open Access article licensed under a Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, sharing, adaptation, distribution and reproduction in any medium or format, for any purpose, even commercially, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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Figure 4. — ABT-199 binding to the BH3 hydrophobic cleft leads to conformational changes on the opposite side of Bcl-2 in the BH4 domain. Representative structures corresponding to the medians of principal structure clusters of the free Bcl-2 (A) or Bcl-2:ABT-199 complex (B) following the ABT-199 binding (in B) and equilibration are shown. Panels show a ribbon representation of the backbone (left) or the CPK-colored surface (right) of the Bcl-2 protein. The BH4 domain is highlighted in yellow, and the adjacent loop is in dark brown. ABT-199 is represented with violet sticks (left) or a semitransparent surface (right). Note a difference in BH4 domain structure (both backbone and exposed surface) as well as adhesion of a part of the loop between BH4 and BH2 domains in the Bcl-2:ABT-199 complex