There are nine members of the Chromodomain, Helicase, DNA-binding (CHD) family. They are characterised by two chromodomains arranged in tandem, N-terminal to the ATPase/helicase domain. Chromodomains are comprised of a β-sheet folded against an α-helix that collectively mediates binding to methyl-lysine residues []. This entry represent chromodomain-helicase-DNA-binding protein 5 (CHD5). CHD5 is almost exclusively expresssed in brain and testis, and is required for spermiogenesis and chromatin condensation []. CHD5 plays a role in the development of the nervous system [, , ]. It has been identified as a tumour suppressor [].
This entry represents the N-terminal domain of CHD (Chromodomain, Helicase, DNA-binding) proteins. CHD3 and CHD4 belong to the class II subfamily of CHD ATPases, and each is present as a core catalytic subunit in separate NuRD complexes, which regulate chromatin organisation and gene transcription []. CHD5 forms a NuRD-type chromatin remodeling complex and acts as a tumour suppressor []. There are nine members of the Chromodomain, Helicase, DNA-binding (CHD) family. They are characterised by two chromodomains arranged in tandem, N-terminal to the ATPase/helicase domain. Chromodomains are comprised of a β-sheet folded against an α-helix that collectively mediates binding to methyl-lysine residues [].
This entry represents the C-terminal domain of CHD (Chromodomain, Helicase, DNA-binding) proteins. CHD3 and CHD4 belong to the class II subfamily of CHD ATPases, and each is present as a core catalytic subunit in separate NuRD complexes, which regulate chromatin organisation and gene transcription []. CHD5 forms a NuRD-type chromatin remodeling complex and acts as a tumour suppressor []. There are nine members of the Chromodomain, Helicase, DNA-binding (CHD) family. They are characterised by two chromodomains arranged in tandem, N-terminal to the ATPase/helicase domain. Chromodomains are comprised of a β-sheet folded against an α-helix that collectively mediates binding to methyl-lysine residues [].
