Your browser doesn't support javascript.
1H, 13C, and 15N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein.
Korn, Sophie M; Lambertz, Roderick; Fürtig, Boris; Hengesbach, Martin; Löhr, Frank; Richter, Christian; Schwalbe, Harald; Weigand, Julia E; Wöhnert, Jens; Schlundt, Andreas.
  • Korn SM; Institute for Molecular Biosciences, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 9, 60438, Frankfurt/M, Germany.
  • Lambertz R; Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-University Frankfurt, 60438, Frankfurt/M, Germany.
  • Fürtig B; Institute for Molecular Biosciences, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 9, 60438, Frankfurt/M, Germany.
  • Hengesbach M; Institute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438, Frankfurt/M, Germany.
  • Löhr F; Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-University Frankfurt, 60438, Frankfurt/M, Germany.
  • Richter C; Institute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438, Frankfurt/M, Germany.
  • Schwalbe H; Institute of Biophysical Chemistry, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 9, 60438, Frankfurt/M, Germany.
  • Weigand JE; Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-University Frankfurt, 60438, Frankfurt/M, Germany.
  • Wöhnert J; Institute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438, Frankfurt/M, Germany.
  • Schlundt A; Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-University Frankfurt, 60438, Frankfurt/M, Germany.
Biomol NMR Assign ; 15(1): 129-135, 2021 04.
Article in English | MEDLINE | ID: covidwho-1141504
Semantic information from SemMedBD (by NLM)
1. Measles Virus Nucleoprotein PART_OF 2019 novel coronavirus
Subject
Measles Virus Nucleoprotein
Predicate
PART_OF
Object
2019 novel coronavirus
2. 2019 novel coronavirus CAUSES Communicable Diseases
Subject
2019 novel coronavirus
Predicate
CAUSES
Object
Communicable Diseases
3. RNA-Binding Proteins AFFECTS Viral Transcription
Subject
RNA-Binding Proteins
Predicate
AFFECTS
Object
Viral Transcription
4. Measles Virus Nucleoprotein INTERACTS_WITH Nucleic Acids
Subject
Measles Virus Nucleoprotein
Predicate
INTERACTS_WITH
Object
Nucleic Acids
5. Measles Virus Nucleoprotein PART_OF 2019 novel coronavirus
Subject
Measles Virus Nucleoprotein
Predicate
PART_OF
Object
2019 novel coronavirus
6. 2019 novel coronavirus CAUSES Communicable Diseases
Subject
2019 novel coronavirus
Predicate
CAUSES
Object
Communicable Diseases
7. RNA-Binding Proteins AFFECTS Viral Transcription
Subject
RNA-Binding Proteins
Predicate
AFFECTS
Object
Viral Transcription
8. Measles Virus Nucleoprotein INTERACTS_WITH Nucleic Acids
Subject
Measles Virus Nucleoprotein
Predicate
INTERACTS_WITH
Object
Nucleic Acids
ABSTRACT
The current outbreak of the highly infectious COVID-19 respiratory disease is caused by the novel coronavirus SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus 2). To fight the pandemic, the search for promising viral drug targets has become a cross-border common goal of the international biomedical research community. Within the international Covid19-NMR consortium, scientists support drug development against SARS-CoV-2 by providing publicly available NMR data on viral proteins and RNAs. The coronavirus nucleocapsid protein (N protein) is an RNA-binding protein involved in viral transcription and replication. Its primary function is the packaging of the viral RNA genome. The highly conserved architecture of the coronavirus N protein consists of an N-terminal RNA-binding domain (NTD), followed by an intrinsically disordered Serine/Arginine (SR)-rich linker and a C-terminal dimerization domain (CTD). Besides its involvement in oligomerization, the CTD of the N protein (N-CTD) is also able to bind to nucleic acids by itself, independent of the NTD. Here, we report the near-complete NMR backbone chemical shift assignments of the SARS-CoV-2 N-CTD to provide the basis for downstream applications, in particular site-resolved drug binding studies.
Subject(s)
Keywords

Full text: Available Collection: International databases Database: MEDLINE Main subject: Magnetic Resonance Spectroscopy / Coronavirus Nucleocapsid Proteins / SARS-CoV-2 Type of study: Randomized controlled trials Language: English Journal: Biomol NMR Assign Journal subject: Molecular Biology / Nuclear Medicine Year: 2021 Document Type: Article Affiliation country: S12104-020-09995-y

Similar

MEDLINE

...
LILACS

LIS


Full text: Available Collection: International databases Database: MEDLINE Main subject: Magnetic Resonance Spectroscopy / Coronavirus Nucleocapsid Proteins / SARS-CoV-2 Type of study: Randomized controlled trials Language: English Journal: Biomol NMR Assign Journal subject: Molecular Biology / Nuclear Medicine Year: 2021 Document Type: Article Affiliation country: S12104-020-09995-y