title: ¹H, ¹³C and ¹⁵N resonance assignments of an N-terminal domain of CHD4.
abstract: Chromatin-remodeling proteins have a pivotal role in normal cell function and development, catalyzing conformational changes in DNA that ultimately result in changes in gene expression patterns. Chromodomain helicase DNA-binding protein 4 (CHD4), the defining subunit of the nucleosome remodeling and deacetylase (NuRD) complex, is a nucleosome-remodeling protein of the SNF2/ISWI2 family, members of which contain two chromo domains and an ATP-dependent helicase module. CHD3, CHD4 and CHD5 also contain two contiguous PHD domains and have an extended N-terminal region that has not previously been characterized. We have identified a stable domain in the N-terminal region of CHD4 and report here the backbone and side chain resonance assignments for this domain at pH 7.5 and 25 °C (BMRB No. 18906).
authors: School of Molecular Bioscience, The University of Sydney, Building G08, Corner Butlin Avenue and Maze Crescent, Sydney, NSW, 2006, Australia, ana.silva@sydney.edu.au.
authors: Ana P G
authors: AP
authors: Silva
authors: Ann H
authors: AH
authors: Kwan
authors: Joel P
authors: JP
authors: Mackay
mesh_terms: D001324:Autoantigens / Q000737:chemistry*; D002247:Carbon Isotopes; D006801:Humans; D006859:Hydrogen; D056245:Mi-2 Nucleosome Remodeling and Deacetylase Complex / Q000737:chemistry*; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D001324:Autoantigens; C115323:CHD4 protein, human; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D006859:Hydrogen; D056245:Mi-2 Nucleosome Remodeling and Deacetylase Complex