2V0E
BRK domain from human CHD7
Summary for 2V0E
| Entry DOI | 10.2210/pdb2v0e/pdb |
| Related | 2CKC 2V0F |
| Descriptor | CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 7 (1 entity in total) |
| Functional Keywords | nucleotide-binding, chromatin regulator, charge syndrome, phosphorylation, disease mutation, transcription regulation, chd7, helicase, hydrolase, brk domain, atp-binding, dna-binding, transcription, nuclear protein |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Isoform 1: Nucleus . Isoform 3: Nucleus, nucleolus : Q9P2D1 |
| Total number of polymer chains | 1 |
| Total formula weight | 6169.90 |
| Authors | Allen, M.D.,Religa, T.L.,Freund, S.M.V.,Bycroft, M. (deposition date: 2007-05-14, release date: 2007-05-22, Last modification date: 2024-05-15) |
| Primary citation | Allen, M.D.,Religa, T.L.,Freund, S.M.V.,Bycroft, M. Solution Structure of the Brk Domains from Chd7 J.Mol.Biol., 371:1135-, 2007 Cited by PubMed Abstract: CHD7 is a member of the chromodomain helicase DNA binding domain (CHD) family of ATP-dependent chromatin remodelling enzymes. It is mutated in CHARGE syndrome, a multiple congenital anomaly condition. CHD7 is one of a subset of CHD proteins, unique to metazoans that contain the BRK domain, a protein module also found in the Brahma/BRG1 family of helicases. We describe here the NMR solution structure of the two BRK domains of CHD7. Each domain has a compact betabetaalphabeta fold. The second domain has a C-terminal extension consisting of two additional helices. The structure differs from those of other domains present in chromatin-associated proteins. PubMed: 17603073DOI: 10.1016/J.JMB.2007.06.007 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
