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1H, 13C, and 15N resonance assignments for the tandem PHD finger motifs of human CHD4
journal contribution
posted on 2023-06-15, 15:41 authored by Louise J Walport, Rosa Morra, Erika ManciniErika Mancini, Christina RedfieldThe 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
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- Published version
Journal
Biomolecular NMR AssignmentsISSN
1874-2718Publisher
Springer VerlagExternal DOI
Issue
2Volume
9Page range
239-242Department affiliated with
- Biochemistry Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2015-01-30First Open Access (FOA) Date
2015-01-30First Compliant Deposit (FCD) Date
2015-01-30Usage metrics
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