Article
Structural studies of human histone deacetylase 8 and its site-specific variants complexed with substrate and inhibitors.
Biochemistry - 23 Dec 2008
Dowling Daniel P, Gantt Stephanie L, Gattis Samuel G, Fierke Carol A, Christianson David W
Abstract excerpt
Metal-dependent histone deacetylases (HDACs) require Zn(2+) or Fe(2+) to regulate the acetylation of lysine residues in histones and other proteins in eukaryotic cells. Isozyme HDAC8 is perhaps the archetypical member of the class I HDAC family and serves as a paradigm for studying structure-function relationships. Here, we report the structures of HDAC8 complexes with trichostatin A and...
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