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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.

Original publication

DOI

10.1021/acs.jmedchem.7b00933

Type

Journal article

Journal

J Med Chem

Publication Date

09/11/2017

Volume

60

Pages

9090 - 9096

Keywords

Binding Sites, Binding, Competitive, Crystallography, X-Ray, Histone Deacetylase 6, Humans, Ligands, Protein Binding, Protein Interaction Domains and Motifs, Ubiquitin, Zinc Fingers