Indirect DNA readout on the protein side: coupling between histidine protonation, global structural cooperativity, dynamics, and DNA binding of the human papillomavirus type 16 E2C domain.

@article{Eliseo2009IndirectDR,
  title={Indirect DNA readout on the protein side: coupling between histidine protonation, global structural cooperativity, dynamics, and DNA binding of the human papillomavirus type 16 E2C domain.},
  author={Tommaso Eliseo and Ignacio E. S{\'a}nchez and Alejandro Daniel Nadra and Mariano Dellarole and Maurizio Paci and Gonzalo de Prat Gay and Daniel O Cicero},
  journal={Journal of molecular biology},
  year={2009},
  volume={388 2},
  pages={327-44}
}
DNA sequence recognition by the homodimeric C-terminal domain of the human papillomavirus type 16 E2 protein (E2C) is known to involve both direct readout and DNA-dependent indirect readout mechanisms, while protein-dependent indirect readout has been deduced but not directly observed. We have investigated coupling between specific DNA binding and the dynamics of the unusual E2C fold, using pH as an external variable. Nuclear magnetic resonance and isothermal titration calorimetry show that pH… CONTINUE READING

References

Publications referenced by this paper.
Showing 1-10 of 80 references

The transition state for protein–DNA recognition

  • D. U. Ferreiro, I. E. Sanchez, G. de Prat Gay
  • Proc. Natl Acad. Sci
  • 2008
Highly Influential
10 Excerpts

Papillomavirus proteins and their potential as drug design targets. FutureMed

  • R. S. Hegde
  • 2006
Highly Influential
3 Excerpts

Similar Papers

Loading similar papers…