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Figure 1

Figure 1. From: A PUMA mechanism unfolds.

Induction of p53-dependent apoptosis by selective PUMABH3-mediated dissociation of the mitochondrial p53–BCL-XL complex. (a) A unique π-stacking interaction between PUMABH3 Trp71 (red) and BCL-XL His113 (blue) triggers partial unfolding of the BCL-XL α2-α3 region (α3*), a component of the previously defined p53 binding site on BCL-XL. BCL-XL residues that undergo the greatest chemical shift change upon PUMABH3 titration are depicted as pink balls, whereas those residues affected by p53 DNA-binding domain engagement, as defined by Petros et al.8, are represented by green balls. Thr115 is dual-colored, reflecting an exemplary residue that is affected both by PUMABH3 (ref. 5) and p53 (ref. 8) binding. The ribbon diagram of BCL-XLΔC protein and the PUMABH3 helix are colored orange and cyan, respectively. (b) Irradiation-induced DNA damage triggers the p53 transcriptional response, resulting in the upregulation of PUMA, among other targets. PUMABH3 engages BCL-XL at the canonical binding site, resulting in structural changes that promote dissociation of p53. This liberation of cytosolic p53 is believed to contribute to p53-dependent apoptosis through amplification of the transcriptional response and direct activation of proapoptotic BAX. Cyt c, cytochrome c.

Loren D Walensky. Nat Chem Biol. ;9(3):141-143.

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