Chromodomain helicase DNA binding protein 3 (CHD3) (CHD3)

Chromodomain helicase DNA binding protein 3 (CHD3) is an ATP-dependent chromatin remodeling enzyme that acts as a core subunit of the Nucleosome Remodeling and Deacetylase (NuRD) complex [1]. It plays a vital role in epigenetic regulation by utilizing the energy from ATP hydrolysis to reposition nucleosomes, which typically leads to transcriptional repression and gene silencing [1, 2]. The specific genetic locus CHD3 c.3073C>T results in a p.Arg1025Trp amino acid substitution within the protein's conserved helicase domain [2]. This pathogenic variant is a primary cause of Snijders Blok-Campeau syndrome, a neurodevelopmental disorder characterized by macrocephaly, speech impairment, and intellectual disability [2, 3]. Although CHD3 is not currently targeted by any FDA-approved small molecules, its central role in the NuRD complex makes it a significant subject of research for developmental biology and potential genetic interventions [1, 3]. Understanding the functional impact of the c.3073C>T mutation is crucial for developing precision therapies aimed at restoring normal chromatin remodeling activity in affected patients [2].

Other names

Mi-2 alphaMi2-ALPHAATP-dependent helicase CHD3ZCH1Mi-2 autoantigen 240 kDa subunithZCH1

CHD3 utilizes the energy from ATP hydrolysis to move, eject, or restructure nucleosomes, thereby regulating the accessibility of DNA to transcriptional machinery [1]. As a core component of the Nucleosome Remodeling and Deacetylase (NuRD) complex, it facilitates histone deacetylation and chromatin condensation to repress gene expression [1, 2].