Histone deacetylase 10: A polyamine deacetylase from the crystal structure to the first inhibitors.
Crystallography
HDAC10
HDAC10 inhibitors
HDAC10 substrates
Polyamine deacetylase
Journal
Current opinion in structural biology
ISSN: 1879-033X
Titre abrégé: Curr Opin Struct Biol
Pays: England
ID NLM: 9107784
Informations de publication
Date de publication:
10 2023
10 2023
Historique:
received:
01
04
2023
revised:
16
06
2023
accepted:
10
07
2023
medline:
18
9
2023
pubmed:
6
8
2023
entrez:
5
8
2023
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 37542907
pii: S0959-440X(23)00142-2
doi: 10.1016/j.sbi.2023.102668
pii:
doi:
Substances chimiques
Polyamines
0
Histone Deacetylases
EC 3.5.1.98
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
102668Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier Ltd.. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.