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

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posted on 2023-06-15, 15:41 authored by Louise J Walport, Rosa Morra, Erika ManciniErika Mancini, Christina Redfield
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.

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Publication status

  • Published

File Version

  • Published version

Journal

Biomolecular NMR Assignments

ISSN

1874-2718

Publisher

Springer Verlag

Issue

2

Volume

9

Page range

239-242

Department affiliated with

  • Biochemistry Publications

Full text available

  • Yes

Peer reviewed?

  • Yes

Legacy Posted Date

2015-01-30

First Open Access (FOA) Date

2015-01-30

First Compliant Deposit (FCD) Date

2015-01-30

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