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NMR assignments of the macro domain from Middle East respiratory syndrome coronavirus (MERS-CoV)

The newly emerging human pathogen, Middle East respiratory syndrome coronavirus (MERS-CoV), contains a macro domain in the highly conserved N-terminal region of non-structural protein 3. Intense research has shown that macro domains bind ADP-ribose and other derivatives, but it still remains intangi...

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Autores principales: Huang, Yi-Ping, Cho, Chao-Cheng, Chang, Chi-Fon, Hsu, Chun-Hua
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7091117/
https://www.ncbi.nlm.nih.gov/pubmed/26993639
http://dx.doi.org/10.1007/s12104-016-9676-9
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author Huang, Yi-Ping
Cho, Chao-Cheng
Chang, Chi-Fon
Hsu, Chun-Hua
author_facet Huang, Yi-Ping
Cho, Chao-Cheng
Chang, Chi-Fon
Hsu, Chun-Hua
author_sort Huang, Yi-Ping
collection PubMed
description The newly emerging human pathogen, Middle East respiratory syndrome coronavirus (MERS-CoV), contains a macro domain in the highly conserved N-terminal region of non-structural protein 3. Intense research has shown that macro domains bind ADP-ribose and other derivatives, but it still remains intangible about their exact function. In this study we report the preliminary structural analysis through solution NMR spectroscopy of the MERS-CoV macro domain. The near complete NMR assignments of MERS-CoV macro domain provide the basis for subsequent structural and biochemical investigation in the context of protein function.
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spelling pubmed-70911172020-03-24 NMR assignments of the macro domain from Middle East respiratory syndrome coronavirus (MERS-CoV) Huang, Yi-Ping Cho, Chao-Cheng Chang, Chi-Fon Hsu, Chun-Hua Biomol NMR Assign Article The newly emerging human pathogen, Middle East respiratory syndrome coronavirus (MERS-CoV), contains a macro domain in the highly conserved N-terminal region of non-structural protein 3. Intense research has shown that macro domains bind ADP-ribose and other derivatives, but it still remains intangible about their exact function. In this study we report the preliminary structural analysis through solution NMR spectroscopy of the MERS-CoV macro domain. The near complete NMR assignments of MERS-CoV macro domain provide the basis for subsequent structural and biochemical investigation in the context of protein function. Springer Netherlands 2016-03-18 2016 /pmc/articles/PMC7091117/ /pubmed/26993639 http://dx.doi.org/10.1007/s12104-016-9676-9 Text en © Springer Science+Business Media Dordrecht 2016 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Article
Huang, Yi-Ping
Cho, Chao-Cheng
Chang, Chi-Fon
Hsu, Chun-Hua
NMR assignments of the macro domain from Middle East respiratory syndrome coronavirus (MERS-CoV)
title NMR assignments of the macro domain from Middle East respiratory syndrome coronavirus (MERS-CoV)
title_full NMR assignments of the macro domain from Middle East respiratory syndrome coronavirus (MERS-CoV)
title_fullStr NMR assignments of the macro domain from Middle East respiratory syndrome coronavirus (MERS-CoV)
title_full_unstemmed NMR assignments of the macro domain from Middle East respiratory syndrome coronavirus (MERS-CoV)
title_short NMR assignments of the macro domain from Middle East respiratory syndrome coronavirus (MERS-CoV)
title_sort nmr assignments of the macro domain from middle east respiratory syndrome coronavirus (mers-cov)
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7091117/
https://www.ncbi.nlm.nih.gov/pubmed/26993639
http://dx.doi.org/10.1007/s12104-016-9676-9
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