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

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dc.contributor.authorK J Kim-
dc.contributor.authorM C Park-
dc.contributor.authorS J Choi-
dc.contributor.authorY S Oh-
dc.contributor.authorE C Choi-
dc.contributor.authorH J Cho-
dc.contributor.authorMyung Hee Kim-
dc.contributor.authorS H Kim-
dc.contributor.authorD W Kim-
dc.contributor.authorS Kim-
dc.contributor.authorB S Kang-
dc.date.accessioned2017-04-19T09:10:15Z-
dc.date.available2017-04-19T09:10:15Z-
dc.date.issued2008-
dc.identifier.issn00219258-
dc.identifier.uri10.1074/jbc.M800859200ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8425-
dc.description.abstractAlthough 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-? resolution and identified its potential sites of interaction with ATM. AIMP3 contains two distinct domains linked by a 7-amino acid (Lys57-Ser63) peptide, which contains a 310 helix. The 56-amino acid N-terminal domain consists of two helices into which three antiparallel β strands are inserted, and the 111-amino acid C-terminal domain contains a bundle of five helices (Thr64-Tyr152) followed by a coiled region (Pro153-Leu169). Structural analyses revealed homologous proteins such as yeast glutamyl-tRNA synthetase, Arc1p, EF1Bγ, and glutathione S-transferase and suggested two potential molecular binding sites. Moreover, mutations at the C-terminal putative binding site abolished the interaction between AIMP3 and ATM and the ability of AIMP3 to activate p53. Thus, this work identified the two potential molecular interaction sites of AIMP3 and determined the residues critical for its tumor-suppressive activity through the interaction with ATM.-
dc.publisherAmer Soc Biochemistry Molecular Biology Inc-
dc.titleDetermination of three-dimensional structure and residues of the novel tumor suppressor AIMP3/p18 required for the interaction with ATM-
dc.title.alternativeDetermination of three-dimensional structure and residues of the novel tumor suppressor AIMP3/p18 required for the interaction with ATM-
dc.typeArticle-
dc.citation.titleJournal of Biological Chemistry-
dc.citation.number20-
dc.citation.endPage14040-
dc.citation.startPage14032-
dc.citation.volume283-
dc.contributor.affiliatedAuthorMyung Hee Kim-
dc.contributor.alternativeName김경진-
dc.contributor.alternativeName박민철-
dc.contributor.alternativeName최소정-
dc.contributor.alternativeName오영선-
dc.contributor.alternativeName최응칠-
dc.contributor.alternativeName조효제-
dc.contributor.alternativeName김명희-
dc.contributor.alternativeName김소현-
dc.contributor.alternativeName김동욱-
dc.contributor.alternativeName김성훈-
dc.contributor.alternativeName강범식-
dc.identifier.bibliographicCitationJournal of Biological Chemistry, vol. 283, no. 20, pp. 14032-14040-
dc.identifier.doi10.1074/jbc.M800859200-
dc.description.journalClassY-
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Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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