Chromodomain helicase DNA-binding protein family (CHD family)

The Chromodomain helicase DNA-binding protein (CHD) family consists of ATP-dependent chromatin remodelers that utilize energy from ATP hydrolysis to reposition nucleosomes, regulate chromatin accessibility, and control gene expression. CHD family proteins (in humans, CHD1 to CHD9) are distinguished by the presence of N-terminal chromodomains, a SNF2-like ATPase domain, and, in some subfamilies, additional domains (e.g., PHD zinc finger, SANT, BRK domains). They play critical roles in embryonic development, stem cell biology, DNA repair, and epigenetic regulation. Mutations in various CHD members are causative in certain neurodevelopmental and developmental disorders and associate with multiple cancers. While not targeted directly by any approved drugs, they are of significant interest for their roles in epigenetic regulation, cancer biology, and developmental disease.

Other names

Chromatin remodeler CHD proteinsChromodomain helicase/ATPase familyCHD1–CHD9 (individual members include, for example, CHD1, CHD2, Mi-2α/CHD3, Mi-2β/CHD4, etc.)

Drugs or therapeutic interventions would most likely act by inhibiting or modulating chromatin remodeling, thereby altering gene expression programs relevant for disease states (e.g., cancer cell proliferation, stem cell fate)