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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Bibliographic Details
Published in:Biomolecular NMR assignments 2016-10, Vol.10 (2), p.245-248
Main Authors: Huang, Yi-Ping, Cho, Chao-Cheng, Chang, Chi-Fon, Hsu, Chun-Hua
Format: Article
Language:English
Subjects:
Biochemistry
Biological and Medical Physics
Biophysics
Coronaviridae
Coronaviruses
Magnetic resonance spectroscopy
Middle East Respiratory Syndrome Coronavirus - chemistry
NMR
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular
Physics
Physics and Astronomy
Polymer Sciences
Protein Domains
Respiratory diseases
Ribose
Viral Nonstructural Proteins - chemistry
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Summary: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.
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-016-9676-9