@article{bibcite_689,
  author = {A. Dalle Vedove and G. Cazzanelli and V. G. D{\textquoteright}Agostino and P. A. Vargas-Rosales and A. Caflisch and G. Lolli},
  title = {Unusual Backfolded Binding Poses of BAZ2A Bromodomain Binders},
  abstract = {<p>BAZ2A is a large multidomain protein overexpressed in aggressive prostate cancer, where it potentiates migration and invasion of other tissues. To counteract its metastasis-promoting role, small molecules interfering with the recognition of acetylated lysines by the BAZ2A bromodomain have been identified. However, unlike other bromodomains, BAZ2A has a shallow pocket, which significantly complicates the development of potent inhibitors. Here, we report the exploration of the acetyl-pyrrole scaffold, leading to the identification of BAZ2A-binding compounds assuming a peculiar, almost enclosed, conformation, as determined by X-ray crystallography. These molecules pose the basis for the development of potent BAZ2A macrocyclic inhibitors, as performed for other bromodomains.</p>},
  year = {2026},
  journal = {Acta Crystallographica Section D, Structural Biology},
  volume = {82},
  pages = {1-9},
  month = {2026 Jul 01},
  url = {https://journals.iucr.org/d/issues/2026/07/00/chr5011/index.html},
  doi = {10.1107/S2059798326004596},
  language = {eng},
}