组蛋白脱乙酰化酶10：从晶体结构到首个抑制剂的多胺脱乙酰酶。
Histone deacetylase 10: A polyamine deacetylase from the crystal structure to the first inhibitors.
发表日期：2023 Aug 03
作者：
Chiara Lambona, Clemens Zwergel, Rossella Fioravanti, Sergio Valente, Antonello Mai
来源：
CURRENT OPINION IN STRUCTURAL BIOLOGY
摘要：
多胺脱乙酰酶活性在40多年前被发现，但是负责这一活性的组蛋白脱乙酰酶10（HDAC10）直到最近才被描述。HDAC10是一个IIb类HDAC，与其最近的亲缘物质α-乙酰化α-小管蛋白酶HDAC6一样。过去两年间，HDAC10因其在疾病特别是癌症中的作用而受到关注。本文综述了化学和结构生物学方法在研究HDAC10方面的应用。我们将阐明近年来对HDAC10复杂结构生物学的理解取得的最新进展，以及第一批高选择性HDAC10抑制剂的发现。版权所有© 2023 作者。由Elsevier Ltd.出版。保留所有权利。
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.Copyright © 2023 The Authors. Published by Elsevier Ltd.. All rights reserved.