6mr5

Publication Abstract from PubMed

Mercaptoacetamide histone deacetylase inhibitors are neuroprotective agents that do not exhibit the genotoxicity associated with more commonly used hydroxamate inhibitors. Here, we present the crystal structure of a selective mercaptoacetamide complexed with the C-terminal catalytic domain of HDAC6. When compared with the structure of a mercaptoacetamide bound to the class I isozyme HDAC8, different interactions are observed with the conserved tandem histidine pair in the active site. These differences likely contribute to the selectivity for inhibition of HDAC6, an important target for cancer chemotherapy and the treatment of neurodegenerative disease.

Molecular Basis for the Selective Inhibition of Histone Deacetylase 6 by a Mercaptoacetamide Inhibitor.,Porter NJ, Shen S, Barinka C, Kozikowski AP, Christianson DW ACS Med Chem Lett. 2018 Nov 21;9(12):1301-1305. doi:, 10.1021/acsmedchemlett.8b00487. eCollection 2018 Dec 13. PMID:30613344^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.