Dataset for the NMR structure of the intrinsically disordered acidic region of XPC bound to the PH domain of TFIIH p62

The global genome nucleotide excision repair factor XPC firstly detects DNA lesions and then recruits a ten-subunit complex TFIIH through binding to the subunit p62 to unwind the damaged DNA for excision repair. This data article contains detailed nuclear magnetic resonance (NMR) restraints (nuclear...

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Autores principales: Okuda, Masahiko, Nishimura, Yoshifumi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Data Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4731421/
https://www.ncbi.nlm.nih.gov/pubmed/26909369
http://dx.doi.org/10.1016/j.dib.2015.12.034
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author Okuda, Masahiko
Nishimura, Yoshifumi
author_facet Okuda, Masahiko
Nishimura, Yoshifumi
author_sort Okuda, Masahiko
collection PubMed
description The global genome nucleotide excision repair factor XPC firstly detects DNA lesions and then recruits a ten-subunit complex TFIIH through binding to the subunit p62 to unwind the damaged DNA for excision repair. This data article contains detailed nuclear magnetic resonance (NMR) restraints (nuclear Overhauser enhancement (NOE)-derived distance restraints, dihedral angle restraints, and hydrogen bond restraints) used for the structure determination of the complex formed between the intrinsically disordered acidic region of XPC and the pleckstrin homology (PH) domain of TFIIH p62, related to the recent work entitled “Structural insight into the mechanism of TFIIH recognition by the acidic string of the nucleotide excision repair factor XPC.” [1].
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spelling pubmed-47314212016-02-23 Dataset for the NMR structure of the intrinsically disordered acidic region of XPC bound to the PH domain of TFIIH p62 Okuda, Masahiko Nishimura, Yoshifumi Data Brief Data Article The global genome nucleotide excision repair factor XPC firstly detects DNA lesions and then recruits a ten-subunit complex TFIIH through binding to the subunit p62 to unwind the damaged DNA for excision repair. This data article contains detailed nuclear magnetic resonance (NMR) restraints (nuclear Overhauser enhancement (NOE)-derived distance restraints, dihedral angle restraints, and hydrogen bond restraints) used for the structure determination of the complex formed between the intrinsically disordered acidic region of XPC and the pleckstrin homology (PH) domain of TFIIH p62, related to the recent work entitled “Structural insight into the mechanism of TFIIH recognition by the acidic string of the nucleotide excision repair factor XPC.” [1]. Elsevier 2016-01-02 /pmc/articles/PMC4731421/ /pubmed/26909369 http://dx.doi.org/10.1016/j.dib.2015.12.034 Text en © 2016 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Data Article
Okuda, Masahiko
Nishimura, Yoshifumi
Dataset for the NMR structure of the intrinsically disordered acidic region of XPC bound to the PH domain of TFIIH p62
title Dataset for the NMR structure of the intrinsically disordered acidic region of XPC bound to the PH domain of TFIIH p62
title_full Dataset for the NMR structure of the intrinsically disordered acidic region of XPC bound to the PH domain of TFIIH p62
title_fullStr Dataset for the NMR structure of the intrinsically disordered acidic region of XPC bound to the PH domain of TFIIH p62
title_full_unstemmed Dataset for the NMR structure of the intrinsically disordered acidic region of XPC bound to the PH domain of TFIIH p62
title_short Dataset for the NMR structure of the intrinsically disordered acidic region of XPC bound to the PH domain of TFIIH p62
title_sort dataset for the nmr structure of the intrinsically disordered acidic region of xpc bound to the ph domain of tfiih p62
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4731421/
https://www.ncbi.nlm.nih.gov/pubmed/26909369
http://dx.doi.org/10.1016/j.dib.2015.12.034
work_keys_str_mv AT okudamasahiko datasetforthenmrstructureoftheintrinsicallydisorderedacidicregionofxpcboundtothephdomainoftfiihp62
AT nishimurayoshifumi datasetforthenmrstructureoftheintrinsicallydisorderedacidicregionofxpcboundtothephdomainoftfiihp62

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