Complementation of RNA binding site mutations in MS2 coat protein heterodimers.

  title={Complementation of RNA binding site mutations in MS2 coat protein heterodimers.},
  author={David S. Peabody and Francis Pol C. Lim},
  journal={Nucleic acids research},
  volume={24 12},
The coat protein of bacteriophage MS2 functions as a symmetric dimer to bind an asymmetric RNA hairpin. This implies the existence of two equivalent RNA binding sites related to one another by a 2-fold symmetry axis. In this view the symmetric binding site defined by mutations conferring the repressor-defective phenotype is a composite picture of these two asymmetric sites. In order to determine whether the RNA ligand interacts with amino acid residues on both subunits of the dimer and in the… CONTINUE READING

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