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

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2014年 / 8卷 / 01期

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

页码：137 / 139

页数：3

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