ArticleActa crystallographica. Section D, Structural biology2026
Unusual backfolded binding poses of BAZ2A bromodomain binders.
Article in Acta crystallographica. Section D, Structural biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
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.
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