1H, 13C and 15N resonance assignments of a C-terminal domain of human CHD1. Mohanty, B., Silva, A., P., G., Mackay, J., P., & Ryan, D., P. Biomolecular NMR Assignments, 10(1):31-34, 4, 2016.
1H, 13C and 15N resonance assignments of a C-terminal domain of human CHD1 [link]Website  abstract   bibtex   
Chromatin remodelling proteins are an essential family of eukaryotic proteins. They harness the energy from ATP hydrolysis and apply it to alter chromatin structure in order to regulate all aspects of genome biology. Chromodomain helicase DNA-binding protein 1 (CHD1) is one such remodelling protein that has specialised nucleosome organising abilities and is conserved across eukaryotes. CHD1 possesses a pair of tandem chromodomains that directly precede the core catalytic Snf2 helicase-like domain, and a C-terminal SANT-SLIDE DNA-binding domain. We have identified an additional conserved domain in the C-terminal region of CHD1. Here, we report the backbone and side chain resonance assignments for this domain from human CHD1 at pH 6.5 and 25 °C (BMRB No. 25638).
@article{
 title = {1H, 13C and 15N resonance assignments of a C-terminal domain of human CHD1},
 type = {article},
 year = {2016},
 identifiers = {[object Object]},
 keywords = {C-terminal domain,CHD1,Chromatin remodelling,Nucleosomes},
 pages = {31-34},
 volume = {10},
 websites = {http://link.springer.com/10.1007/s12104-015-9631-1},
 month = {4},
 day = {19},
 id = {8b6b4b43-87d3-373b-9cda-54046a233f4d},
 created = {2020-10-01T06:20:11.575Z},
 file_attached = {false},
 profile_id = {45e2f77d-7a48-31e0-99de-4a07a154b051},
 group_id = {c2dc1a38-fc29-3f20-8d91-e4e1a13d85ae},
 last_modified = {2020-10-29T21:44:39.549Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {true},
 hidden = {false},
 citation_key = {Mohanty2016a},
 source_type = {ARTICLE},
 notes = {cited By 1},
 private_publication = {false},
 abstract = {Chromatin remodelling proteins are an essential family of eukaryotic proteins. They harness the energy from ATP hydrolysis and apply it to alter chromatin structure in order to regulate all aspects of genome biology. Chromodomain helicase DNA-binding protein 1 (CHD1) is one such remodelling protein that has specialised nucleosome organising abilities and is conserved across eukaryotes. CHD1 possesses a pair of tandem chromodomains that directly precede the core catalytic Snf2 helicase-like domain, and a C-terminal SANT-SLIDE DNA-binding domain. We have identified an additional conserved domain in the C-terminal region of CHD1. Here, we report the backbone and side chain resonance assignments for this domain from human CHD1 at pH 6.5 and 25 °C (BMRB No. 25638).},
 bibtype = {article},
 author = {Mohanty, Biswaranjan and Silva, Ana P. G. and Mackay, Joel P. and Ryan, Daniel P.},
 journal = {Biomolecular NMR Assignments},
 number = {1}
}
Downloads: 0