fig3

The interplay between DNA topoisomerase 2α post-translational modifications and drug resistance

Figure 3. Distribution of the post-translational modifications on the structures of Top2α catalytic domains. A: modifications found in normal homeostasis cells (Bedez et al.[16], 2018) reported on the ATPase domain structure (PDBID: 1ZXM) (top) and DNA binding/cleavage domain (PDBID: 5GWK) (bottom). B: modifications found in cancer cells reported in the PhosphoSitePlus database reported on the catalytic domains. The C-terminal domains for which no structure is available are not represented. Modifications appear as a blue sphere for acetylation, red for phosphorylation and yellow for ubiquitination. Positions that were found either ubiquitinated or SUMOylated appear as pale green spheres. Positions that were found either ubiquitinated or acetylated appear as pale blue spheres. Half of the SUMOylations were identified in the TOPRIM domain and C-gate. Only one position at residue 625 was found solely SUMOylated (dark green) and residue 1196 was found to be the site of acetylation, SUMOylation, and ubiquitination (orange). Positions specifically mentioned in the main text are indicated by a black line. Figures were generated using PyMOL Molecular Graphics System, Version 2.0 Schrödinger, LLC. TOPRIM: topoisomerase-primase domain

Cancer Drug Resistance
ISSN 2578-532X (Online)

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