Conformational dynamics of wild-type Lys-48-linked diubiquitin in solution.

@article{Hirano2011ConformationalDO,
  title={Conformational dynamics of wild-type Lys-48-linked diubiquitin in solution.},
  author={Takashi Hirano and Olivier Serve and Maho Yagi-Utsumi and Emi Takemoto and Takeshi Hiromoto and Tadashi Satoh and Tsunehiro Mizushima and Koichi Kato},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 43},
  pages={37496-502}
}
Proteasomal degradation is mediated through modification of target proteins by Lys-48-linked polyubiquitin (polyUb) chain, which interacts with several binding partners in this pathway through hydrophobic surfaces on individual Ub units. However, the previously reported crystal structures of Lys-48-linked diUb exhibit a closed conformation with sequestered hydrophobic surfaces. NMR studies on mutated Lys-48-linked diUb indicated a pH-dependent conformational equilibrium between closed and open… CONTINUE READING

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