The crystal structure of arginyl-tRNA synthetase from Homo sapiens

Hyun Sook Kim, So Young Cha, Chang Hwa Jo, Ahreum Han, Kwang Yeon Hwang

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)


Arginyl-tRNA synthetase (ArgRS) is a tRNA-binding protein that catalyzes the esterification of l-arginine to its cognate tRNA. l-Canavanine, a structural analog of l-arginine, has recently been studied as an anticancer agent. Here, we determined the crystal structures of the apo, l-arginine-complexed, and l-canavanine-complexed forms of the cytoplasmic free isoform of human ArgRS (hArgRS). Similar interactions were formed upon binding to l-canavanine or l-arginine, but the interaction between Tyr312 and the oxygen of the oxyguanidino group was a little bit different. Detailed conformational changes that occur upon substrate binding were explained. The hArgRS structure was also compared with previously reported homologue structures. The results presented here may provide a basis for the design of new anticancer drugs, such as l-canavanine analogs.

Original languageEnglish
Pages (from-to)2328-2334
Number of pages7
JournalFEBS Letters
Issue number14
Publication statusPublished - 2014 Jun 27


  • Arginyl-tRNA synthetase
  • Enzyme Commission number (
  • Rossmann fold
  • l-Arginine
  • l-Canavanine

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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