Effect of C-terminal mutations of alfalfa mosaic virus coat protein on dimer formation and assembly in vitro.

@article{Choi1999EffectOC,
  title={Effect of C-terminal mutations of alfalfa mosaic virus coat protein on dimer formation and assembly in vitro.},
  author={Jiwon Choi and L. Sue Loesch-Fries},
  journal={Virology},
  year={1999},
  volume={260 1},
  pages={182-9}
}
The coat protein (CP) of alfalfa mosaic virus (AMV) strain 425 assembles to bacilliform or rod-shaped particles in the presence of nucleic acids or to T = 1 empty icosahedral particles in the absence of nucleic acids. To study the determinants of CP assembly, recombinant CPs (rCPs) that contained a (His)(6) region were expressed in Escherichia coli. Wt rCP and a mutant rCP, which lacked the last nine amino acids of the C terminus (amino acids 213-221), assembled to particles that were identical… CONTINUE READING

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