The catalytic domain of free or ligand bound histone deacetylase 4 occurs in solution predominantly in closed conformation.

ABSTRACT: Human histone deacetylase 4 (HDAC4) is a key epigenetic regulator involved in a number of important cellular processes. This makes HDAC4 a promising target for the treatment of several cancers and neurodegenerative diseases, in particular Huntington's disease. HDAC4 is highly regulated by phosphorylation and oxidation, which determine its nuclear or cytosolic localization, and exerts its function through multiple interactions with other proteins, forming multiprotein complexes of varying composition. The catalytic domain of HDAC4 is known to interact with the SMRT/NCOR corepressor complex when the structural zinc-binding domain (sZBD) is intact and forms a closed conformation. Crystal structures of the HDAC4 catalytic domain have been reported showing an open conformation of HDAC4 when bou

SUBMITTER: Schweipert M 

PROVIDER: S-EPMC10868454 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature