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Journal article

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

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...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1007/s12104-014-9582-y

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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More from this funder
Funding agency for:
Mancini, E
Grant:
G0700762/1
More from this funder
Funding agency for:
Mancini, E
Grant:
G0700762/1
Wellcome Trust More from this funder
Publisher:
Springer Netherlands Publisher's website
Journal:
Biomolecular NMR assignments Journal website
Volume:
9
Issue:
2
Pages:
239-242
Publication date:
2015-10-01
DOI:
EISSN:
1874-270X
ISSN:
1874-2718
Language:
English
Keywords:
Pubs id:
pubs:487275
UUID:
uuid:387e5d87-9728-4cf7-8c76-6e22387c963c
Local pid:
pubs:487275
Source identifiers:
487275
Deposit date:
2014-10-23

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