1H, 13C, and 15N resonance assignments for the tandem PHD finger motifs of human CHD4

Walport, Louise J, Morra, Rosa, Mancini, Erika J and Redfield, Christina (2014) 1H, 13C, and 15N resonance assignments for the tandem PHD finger motifs of human CHD4. Biomolecular NMR Assignments. ISSN 1874-2718

[img]
Preview
PDF - Published Version
Download (307kB) | Preview

Abstract

The plant homeodomain (PHD) zinc finger is a structural motif of about 40–60 amino acid residues found in many eukaryotic proteins that are involved in chromatin-mediated gene regulation. The human chromodomain helicase DNA binding protein 4 (CHD4) is a multi-domain protein that harbours, at its N-terminal end, a pair of PHD finger motifs (dPHD) connected by a ~30 amino acid linker. This tandem PHD motif is thought to be involved in targeting CHD4 to chromatin via its interaction with histone tails. Here we report the 1H, 13C and 15N backbone and side-chain resonance assignment of the entire dPHD by heteronuclear multidimensional NMR spectroscopy. These assignments provide the starting point for the determination of the structure, dynamics and histone-binding properties of this tandem domain pair.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Subjects: Q Science
Depositing User: Tom Gittoes
Date Deposited: 30 Jan 2015 11:43
Last Modified: 31 Mar 2017 13:17
URI: http://sro.sussex.ac.uk/id/eprint/52547

View download statistics for this item

📧 Request an update