Abstract
Histone deacetylases (HDACs) are enzymes that cleave acetyl groups from acetyl-lysine residues in histones and various nonhistone proteins. Unlike the other three of the four classes of HDACs that have been identified in humans, which are zinc-dependent amidohydrolases, class III HDACs depend on nicotinamide adenine dinucleotide (NAD+) for their catalytic activity and are named sirtuins. Sirtuin inhibitors have been critical for the linkage of sirtuin activity to many physiological and pathological processes, and sirtuin activity has been associated with the pathogenesis of cancer, HIV, and metabolic and neurological diseases. Presented here is an overview of the solved crystal structures of sirtuin subtypes in complex with inhibitors, substrates, and activators. The chapter also covers computer-based studies that resulted in the design and screening of novel sirtuin inhibitors representing useful chemical probes for studying the biological role of sirtuin isoforms.
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