Determination of three-dimensional structure and residues of the novel tumor suppressor AIMP3/p18 required for the interaction with ATM.

@article{Kim2008DeterminationOT,
  title={Determination of three-dimensional structure and residues of the novel tumor suppressor AIMP3/p18 required for the interaction with ATM.},
  author={Kyung-Jin Kim and Min Chul Park and So Jung Choi and Young Sun Oh and E I Choi and Hyo Je Cho and Myung Hee Kim and Soo-Hyun Kim and Dong Wook Kim and Sunghoon Kim and Beom Sik Kang},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 20},
  pages={14032-40}
}
Although AIMP3/p18 is normally associated with the multi-tRNA synthetase complex via its specific interaction with methionyl-tRNA synthetase, it also works as a tumor suppressor by interacting with ATM, the upstream kinase of p53. To understand the molecular interactions of AIMP3 and the mechanisms involved, we determined the crystal structure of AIMP3 at 2.0-angstroms resolution and identified its potential sites of interaction with ATM. AIMP3 contains two distinct domains linked by a 7-amino… CONTINUE READING