Human HDAC2 in complex with SAHA (vorinostat)

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Histone deacetylases (HDACs) accelerate the hydrolysis of acetylated lysine residues in histones and non-histone proteins. Acetylation removal from lysine-rich histone tails leads to chromatin compaction and transcription repression. Imbalances in HDAC activity have been linked to various diseases, including cancer. HDAC inhibitors can block transformed cell proliferation in vitro and tumour growth in vivo by triggering cell cycle arrest, differentiation, and/or cell death. These anti-proliferative and cytotoxic effects result from an accumulation of acetylated histones, transcription factors, and proteins that regulate proliferation, migration, and cell death. SAHA (suberoylanilide hydroxamic acid), a competitive and reversible inhibitor of class I and II HDACs, is approved for treating cutaneous T-cell lymphoma. This model shows the interactions between HDAC2, a zinc-dependent class I HDAC, and SAHA.