1H, 13C and 15N resonance assignments of an N-terminal domain of CHD4. Silva, A., Kwan, A., & Mackay, J. Biomolecular NMR Assignments, 8(1):137-139, Kluwer Academic Publishers, 2014. cited By 1
1H, 13C and 15N resonance assignments of an N-terminal domain of CHD4 [link]Paper  doi  abstract   bibtex   
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). © 2013 Springer Science+Business Media Dordrecht.
@ARTICLE{Silva2014137,
author={Silva, A.P.G. and Kwan, A.H. and Mackay, J.P.},
title={1H, 13C and 15N resonance assignments of an N-terminal domain of CHD4},
journal={Biomolecular NMR Assignments},
year={2014},
volume={8},
number={1},
pages={137-139},
doi={10.1007/s12104-013-9469-3},
note={cited By 1},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84897113392&doi=10.1007%2fs12104-013-9469-3&partnerID=40&md5=a6b05cf067f1f03e2dab6a552a36c60f},
affiliation={School of Molecular Bioscience, University of Sydney, Building G08, Corner Butlin Avenue and Maze Crescent, Sydney, NSW 2006, Australia},
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). © 2013 Springer Science+Business Media Dordrecht.},
author_keywords={CHD4;  Chromatin remodeling;  N-terminal domain;  NuRD complex;  PAR-binding motif},
keywords={autoantigen;  carbon;  CHD4 protein, human;  histone deacetylase;  hydrogen;  nitrogen, article;  chemistry;  human;  nuclear magnetic resonance;  protein secondary structure;  protein tertiary structure, Autoantigens;  Carbon Isotopes;  Humans;  Hydrogen;  Mi-2 Nucleosome Remodeling and Deacetylase Complex;  Nitrogen Isotopes;  Nuclear Magnetic Resonance, Biomolecular;  Protein Structure, Secondary;  Protein Structure, Tertiary},
correspondence_address1={Silva, A.P.G.; School of Molecular Bioscience, University of Sydney, Building G08, Corner Butlin Avenue and Maze Crescent, Sydney, NSW 2006, Australia; email: ana.silva@sydney.edu.au},
publisher={Kluwer Academic Publishers},
issn={18742718},
pubmed_id={23417793},
language={English},
abbrev_source_title={Biomol. NMR Assignments},
document_type={Article},
source={Scopus},
}

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