1H, 13C and 15N resonance assignments of an N-terminal domain of CHD4

被引:1
|
作者
Silva, Ana P. G. [1 ]
Kwan, Ann H. [1 ]
Mackay, Joel P. [1 ]
机构
[1] Univ Sydney, Sch Mol Biosci, Sydney, NSW 2006, Australia
基金
英国医学研究理事会; 澳大利亚国家健康与医学研究理事会;
关键词
CHD4; Chromatin remodeling; NuRD complex; N-terminal domain; PAR-binding motif; DNA-BINDING DOMAIN; COMPLEX; PROGRESSION; NMR;
D O I
10.1007/s12104-013-9469-3
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
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 A degrees C (BMRB No. 18906).
引用
收藏
页码:137 / 139
页数:3
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