The role of arginine-rich motif and beta-annulus in the assembly and stability of Sesbania mosaic virus capsids.

@article{Satheshkumar2005TheRO,
  title={The role of arginine-rich motif and beta-annulus in the assembly and stability of Sesbania mosaic virus capsids.},
  author={Panayampalli Subbian Satheshkumar and Gudivada Lokesh and Mathur R N Murthy and Handanahal Subbarao Savithri},
  journal={Journal of molecular biology},
  year={2005},
  volume={353 2},
  pages={447-58}
}
Sesbania mosaic virus (SeMV) capsids are stabilized by protein-protein, protein-RNA and calcium-mediated protein-protein interactions. The N-terminal random domain of SeMV coat protein (CP) controls RNA encapsidation and size of the capsids and has two important motifs, the arginine-rich motif (ARM) and the beta-annulus structure. Here, mutational analysis of the arginine residues present in the ARM to glutamic acid was carried out. Mutation of all the arginine residues in the ARM almost… CONTINUE READING
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