Solution Structure of the BRK Domains from CHD7
| Autor: | Tomasz L. Religa, Mark Bycroft, Stefan M.V. Freund, Mark D. Allen |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Protein Folding
Magnetic Resonance Spectroscopy HMG-box Protein Conformation Molecular Sequence Data Molecular Conformation Computational biology Biology Ligands Protein Structure Secondary Chromodomain Protein structure Structural Biology Animals Humans Amino Acid Sequence Molecular Biology Glutathione Transferase Genetics DNA Helicases Helicase Protein Structure Tertiary Chromatin DNA-Binding Proteins Drosophila melanogaster biology.protein Protein folding Heteronuclear single quantum coherence spectroscopy Protein Binding Binding domain |
| Zdroj: | Journal of Molecular Biology. 371:1135-1140 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/j.jmb.2007.06.007 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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