AI Article Synopsis
- Inhibitors of HDAC6 show promise for treating various cancers, focusing on the protein's specific domains.
- Researchers have explored the unique zinc-finger ubiquitin-binding domain (Zf-UBD) of HDAC6 as a potential new target for drug development.
- The study utilized X-ray crystallography and biophysical methods to discover small molecules that bind to the Zf-UBD, identifying two pockets for ligand attachment and introducing the first functional ligands for this domain.
Article Abstract
Inhibitors of HDAC6 have attractive potential in numerous cancers. HDAC6 inhibitors to date target the catalytic domains, but targeting the unique zinc-finger ubiquitin-binding domain (Zf-UBD) of HDAC6 may be an attractive alternative strategy. We developed X-ray crystallography and biophysical assays to identify and characterize small molecules capable of binding to the Zf-UBD and competing with ubiquitin binding. Our results revealed two adjacent ligand-able pockets of HDAC6 Zf-UBD and the first functional ligands for this domain.
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| http://dx.doi.org/10.1021/acs.jmedchem.7b00933 | DOI Listing |
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