Encapsidation of SARS coronavirus genomic RNA

Stable Identifier
Reaction [binding]
Homo sapiens
Related Species
Human SARS coronavirus
Locations in the PathwayBrowser
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The final ribonucleoprotein complex is a hollow helical structure with an approximate diameter of 9-16nm, with the C-terminal domain of N protein forming the inner core and the N-terminal domain forming the outer surface (Neuman et al, 2006; Chen et al, 2007). Oliomerization of the N protein capsid coat is likely nucleated through both protein-RNA and protein-protein interactions by the first few N-protein dimers on the genomic RNA (Saikatendu et al, 2007; Chang et al, 2013; reviewed in Chang et al, 2014). Each N dimer may make contact with up to 7 bases of the RNA (reviewed in Chang et al, 2014).
Literature References
PubMed ID Title Journal Year
23717688 Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging

Chang, CK, Chiang, MH, Chen, CM, Hsu, YL, Huang, TH

PLoS ONE 2013
16873249 Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy

Neuman, BW, Buchmeier, MJ, Milligan, RA, Yeager, M, Adair, BD, Orca, G, Kuhn, P, Yoshioka, C, Quispe, JD

J. Virol. 2006
24418573 The SARS coronavirus nucleocapsid protein--forms and functions

Chang, CK, Hsiao, CD, Hou, MH, Chang, CF, Huang, TH

Antiviral Res. 2014
17229691 Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein

Subramanian, V, Neuman, BW, Saikatendu, KS, Buchmeier, MJ, Joseph, JS, Kuhn, P, Stevens, RC

J. Virol. 2007
17379242 Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA

Riang, L, Chang, CK, Hsiao, CD, Sue, SC, Chen, CY, Bai, HI, Huang, TH, Chang, YW

J. Mol. Biol. 2007
Orthologous Events
Name Identifier Synonyms
severe acute respiratory syndrome DOID:2945 SARS-CoV infection, SARS
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