(1)H, (13)C, and (15)N resonance assignments for the tandem PHD finger motifs of human CHD4.
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-t...
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Format: | Journal article |
Language: | English |
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Springer Netherlands
2015
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author | Walport, L Morra, R Mancini, E Redfield, C |
author_facet | Walport, L Morra, R Mancini, E Redfield, C |
author_sort | Walport, L |
collection | OXFORD |
description | 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 (1)H, (13)C and (15)N 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. |
first_indexed | 2024-03-06T20:53:47Z |
format | Journal article |
id | oxford-uuid:387e5d87-9728-4cf7-8c76-6e22387c963c |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-06T20:53:47Z |
publishDate | 2015 |
publisher | Springer Netherlands |
record_format | dspace |
spelling | oxford-uuid:387e5d87-9728-4cf7-8c76-6e22387c963c2022-03-26T13:50:23Z(1)H, (13)C, and (15)N resonance assignments for the tandem PHD finger motifs of human CHD4.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:387e5d87-9728-4cf7-8c76-6e22387c963cEnglishSymplectic Elements at OxfordSpringer Netherlands2015Walport, LMorra, RMancini, ERedfield, CThe 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 (1)H, (13)C and (15)N 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. |
spellingShingle | Walport, L Morra, R Mancini, E Redfield, C (1)H, (13)C, and (15)N resonance assignments for the tandem PHD finger motifs of human CHD4. |
title | (1)H, (13)C, and (15)N resonance assignments for the tandem PHD finger motifs of human CHD4. |
title_full | (1)H, (13)C, and (15)N resonance assignments for the tandem PHD finger motifs of human CHD4. |
title_fullStr | (1)H, (13)C, and (15)N resonance assignments for the tandem PHD finger motifs of human CHD4. |
title_full_unstemmed | (1)H, (13)C, and (15)N resonance assignments for the tandem PHD finger motifs of human CHD4. |
title_short | (1)H, (13)C, and (15)N resonance assignments for the tandem PHD finger motifs of human CHD4. |
title_sort | 1 h 13 c and 15 n resonance assignments for the tandem phd finger motifs of human chd4 |
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