1ssk

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Structure of the N-terminal RNA-binding Domain of the SARS CoV Nucleocapsid Protein

Structural highlights

1ssk is a 1 chain structure with sequence from Severe acute respiratory syndrome-related coronavirus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NCAP_SARS Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication (PubMed:17210170). May modulate transforming growth factor-beta signaling by binding host SMAD3 (PubMed:18055455).[HAMAP-Rule:MF_04096][1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The severe acute respiratory syndrome (SARS) virus belongs to the Coronaviridea family of viruses. Its virion encodes several proteins including a replicase and four structural proteins. Here we describe the three-dimensional structure of the N-terminal domain of the SARS coronavirus (CoV) nucleocapsid protein. The protein consists of a five-stranded beta sheet with a folding topology distinct from other RNA-binding proteins. Single-stranded RNAs bind to the protein surface at the junction between a flexible, positively charged beta hairpin and the core structure. NMR-based screening was used to identify low molecular weight compounds that bind to this site.

Structure of the N-terminal RNA-binding domain of the SARS CoV nucleocapsid protein.,Huang Q, Yu L, Petros AM, Gunasekera A, Liu Z, Xu N, Hajduk P, Mack J, Fesik SW, Olejniczak ET Biochemistry. 2004 May 25;43(20):6059-63. PMID:15147189[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
31 reviews cite this structure
The molecular biology of coronaviruses.
Masters et al. (2006)
30 more
109 other articles
No citations found

See Also

References

  1. ↑ Stertz S, Reichelt M, Spiegel M, Kuri T, Martínez-Sobrido L, García-Sastre A, Weber F, Kochs G. The intracellular sites of early replication and budding of SARS-coronavirus. Virology. 2007 May 10;361(2):304-15. PMID:17210170 doi:10.1016/j.virol.2006.11.027
  2. ↑ Zhao X, Nicholls JM, Chen YG. Severe acute respiratory syndrome-associated coronavirus nucleocapsid protein interacts with Smad3 and modulates transforming growth factor-beta signaling. J Biol Chem. 2008 Feb 8;283(6):3272-3280. PMID:18055455 doi:10.1074/jbc.M708033200
  3. ↑ Huang Q, Yu L, Petros AM, Gunasekera A, Liu Z, Xu N, Hajduk P, Mack J, Fesik SW, Olejniczak ET. Structure of the N-terminal RNA-binding domain of the SARS CoV nucleocapsid protein. Biochemistry. 2004 May 25;43(20):6059-63. PMID:15147189 doi:10.1021/bi036155b

Contents


PDB ID 1ssk

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