Solution structure of ASPP2 N-terminal domain (N-ASPP2) reveals a ubiquitin-like fold.

@article{Tidow2007SolutionSO,
  title={Solution structure of ASPP2 N-terminal domain (N-ASPP2) reveals a ubiquitin-like fold.},
  author={Henning Tidow and Antonina Andreeva and Trevor J. Rutherford and A. R. Fersht},
  journal={Journal of molecular biology},
  year={2007},
  volume={371 4},
  pages={948-58}
}
Proteins of the ASPP family bind to p53 and regulate p53-mediated apoptosis. Two family members, ASPP1 and ASPP2, have pro-apoptotic functions while iASPP shows anti-apoptotic responses. However, both the mechanism of enhancement/repression of apoptosis and the molecular basis for their different responses remain unknown. To address the role of the N-termini of pro-apoptotic ASPP proteins, we solved the solution structure of N-ASPP2 (1-83) by NMR spectroscopy. The structure of this domain… CONTINUE READING
14 Citations
79 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 14 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 79 references

Similar Papers

Loading similar papers…