1H, 13C and 15N resonance assignments of a C-terminal domain of human CHD1

被引：1

作者：

Mohanty, Biswaranjan ^{[1
,2
]}

Silva, Ana P. G. ^{[1
]}

Mackay, Joel P. ^{[1
]}

Ryan, Daniel P. ^{[3
]}

机构：

[1] Univ Sydney, Sch Mol Biosci, Bldg G08,Corner Butlin Ave & Maze Crescent, Sydney, NSW 2006, Australia

[2] Australian Natl Univ, John Curtin Sch Med Res, Dept Genome Sci, Bldg 131,Garran Rd, Canberra, ACT 2601, Australia

[3] Monash Univ, Monash Inst Pharmaceut Sci, Fac Pharm & Pharmaceut Sci, Med Chem, 381 Royal Parade, Melbourne, Vic 3052, Australia

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2016年 / 10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：

CHD1; Chromatin remodelling; C-terminal domain; Nucleosomes; CHROMATIN; PROTEINS;

D O I：

10.1007/s12104-015-9631-1

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Chromatin remodelling proteins are an essential family of eukaryotic proteins. They harness the energy from ATP hydrolysis and apply it to alter chromatin structure in order to regulate all aspects of genome biology. Chromodomain helicase DNA-binding protein 1 (CHD1) is one such remodelling protein that has specialised nucleosome organising abilities and is conserved across eukaryotes. CHD1 possesses a pair of tandem chromodomains that directly precede the core catalytic Snf2 helicase-like domain, and a C-terminal SANT-SLIDE DNA-binding domain. We have identified an additional conserved domain in the C-terminal region of CHD1. Here, we report the backbone and side chain resonance assignments for this domain from human CHD1 at pH 6.5 and 25 A degrees C (BMRB No. 25638).

引用

页码：31 / 34

页数：4

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