Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities.

@article{Wang2003HexamerizationOP,
  title={Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities.},
  author={Qing Wang and Changcheng Song and Chou-chi Li},
  journal={Biochemical and biophysical research communications},
  year={2003},
  volume={300 2},
  pages={253-60}
}
The 97-kDa valosin-containing protein (p97-VCP or VCP), a hexameric AAA ATPase, plays an important role in diverse cell activities, including ubiquitin-proteasome mediated protein degradation. In this report, we studied dissociation-reassembly kinetics to analyze the structure-function relationship in VCP. Urea-dissociated VCP can reassemble by itself, but addition of ATP, ADP, or ATP-gamma S accelerates the reassembly. Mutation in the ATP-binding site of D1, but not D2, domain abolishes the… CONTINUE READING

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