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Article

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

The Journal of biological chemistry - 16 May 2008

Kim Kyung-Jin, Park Min Chul, Choi So Jung, Oh Young Sun, Choi Eung-Chil, Cho Hyo Je, Kim Myung Hee, Kim Soo-Hyun, Kim Dong Wook, Kim Sunghoon, Kang Beom Sik

Abstract excerpt

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...

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Source

Identifiers

PMID: 18343821
DOI: 10.1074/jbc.M800859200

Genes

ATM

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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