File:Functional domains of the CHD subfamily of ATP-dependent chromatin remodellers .png

English: The unique N-terminal domain of the CDH subfamily contains two chromodomains. The two lobe domains act in tandem as the translocase domain (Tr) and are connected by a peptide linker. NegC* (similar to NegC in ISWI) acts as an inhibitor to lobe movement and translocation until proper binding of the DNA-binding domain (DBD) occurs. NegC* acts by blocking ATP hydrolysis at the lobes. The DBD also acts as a nucleotide ruler, evenly spacing nucleosomes from one another. Post-DNA binding, the DBD causes tension on the DNA strand resulting in a conformational change that blocks regular NegC* inhibition. This allows for the activation of the TR domain, resulting in DNA translocation.