NMR assignments of the macro domain from Middle East respiratory syndrome coronavirus (MERS-CoV).
Identifieur interne : 001202 ( PubMed/Curation ); précédent : 001201; suivant : 001203NMR assignments of the macro domain from Middle East respiratory syndrome coronavirus (MERS-CoV).
Auteurs : Yi-Ping Huang [Taïwan] ; Chao-Cheng Cho [Taïwan] ; Chi-Fon Chang [Taïwan] ; Chun-Hua Hsu [Taïwan]Source :
- Biomolecular NMR assignments [ 1874-270X ] ; 2016.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Viral Nonstructural Proteins.
- chemistry : Middle East Respiratory Syndrome Coronavirus.
- Nuclear Magnetic Resonance, Biomolecular, Protein Domains.
Abstract
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.
DOI: 10.1007/s12104-016-9676-9
PubMed: 26993639
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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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26993639</PMID><DateCompleted><Year>2017</Year><Month>10</Month><Day>24</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1874-270X</ISSN><JournalIssue CitedMedium="Internet"><Volume>10</Volume><Issue>2</Issue><PubDate><Year>2016</Year><Month>10</Month></PubDate></JournalIssue><Title>Biomolecular NMR assignments</Title><ISOAbbreviation>Biomol NMR Assign</ISOAbbreviation></Journal><ArticleTitle>NMR assignments of the macro domain from Middle East respiratory syndrome coronavirus (MERS-CoV).</ArticleTitle><Pagination><MedlinePgn>245-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s12104-016-9676-9</ELocationID><Abstract><AbstractText>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. 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