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).
Chang, CK, Chiang, MH, Chen, CM, Hsu, YL, Huang, TH
Neuman, BW, Buchmeier, MJ, Milligan, RA, Yeager, M, Adair, BD, Orca, G, Kuhn, P, Yoshioka, C, Quispe, JD
Chang, CK, Hsiao, CD, Hou, MH, Chang, CF, Huang, TH
Subramanian, V, Neuman, BW, Saikatendu, KS, Buchmeier, MJ, Joseph, JS, Kuhn, P, Stevens, RC
Riang, L, Chang, CK, Hsiao, CD, Sue, SC, Chen, CY, Bai, HI, Huang, TH, Chang, YW
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