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

## TL;DR

This paper provides detailed NMR resonance assignments for the tandem PHD finger motifs of the human CHD4 protein, aiding in understanding its structure and function in chromatin regulation.

## Contribution

The study presents the first comprehensive NMR resonance assignments for the tandem PHD finger motifs of CHD4.

## Key findings

- 1H, 13C, and 15N resonance assignments were achieved for the entire dPHD of CHD4.
- The assignments will enable structural and functional studies of the tandem PHD motif.
- The work supports future investigations into how CHD4 interacts with chromatin.

## 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.