组蛋白去乙酰化酶 10：从晶体结构到首个抑制剂的多胺去乙酰酶。
Histone deacetylase 10: A polyamine deacetylase from the crystal structure to the first inhibitors.
机构信息
Department of Drug Chemistry and Technologies, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Rome, Italy.
Department of Drug Chemistry and Technologies, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Rome, Italy.
出版信息
Curr Opin Struct Biol. 2023 Oct;82:102668. doi: 10.1016/j.sbi.2023.102668. Epub 2023 Aug 4.
Polyamine deacetylase activity was discovered more than 40 years ago, but the responsible histone deacetylase 10 (HDAC10) was described only recently. HDAC10 is a class IIb HDAC, as is its closest relative, the α-tubulin deacetylase HDAC6. HDAC10 has attracted attention over the last 2 years due to its role in diseases, especially cancer. This review summarises chemical and structural biology approaches to the study of HDAC10. Light will be shed on recent advances in understanding the complex structural biology of HDAC10 and the discovery of the first highly selective HDAC10 inhibitors.
多胺脱乙酰酶活性在 40 多年前被发现，但负责的组蛋白脱乙酰酶 10（HDAC10）直到最近才被描述。HDAC10 是一种 IIb 类 HDAC，与其最接近的亲缘蛋白是α-微管蛋白脱乙酰酶 HDAC6。由于在疾病（特别是癌症）中的作用，HDAC10 在过去 2 年中引起了关注。本文综述了用于研究 HDAC10 的化学和结构生物学方法。本文将重点介绍在理解 HDAC10 复杂结构生物学方面的最新进展，以及首次发现的高度选择性 HDAC10 抑制剂。
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