Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR

Hye Young Cho, Ameeq Ul Mushtaq, Jin Young Lee, Dae Gyu Kim, Min Sook Seok, Minseok Jang, Byung Woo Han, Sunghoon Kim, Young Ho Jeon

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Lysyl-tRNA synthetase (KRS) interacts with the laminin receptor (LR/RPSA) and enhances laminin-induced cell migration in cancer metastasis. In this nuclear magnetic resonance (NMR)-based study, we show that the anticodon-binding domain of KRS binds directly to the C-terminal region of 37LRP, and the previously found inhibitors BC-K-01 and BC-K-YH16899 interfere with KRS-37LRP binding. In addition, the anticodon-binding domain of KRS binds to laminin, observed by NMR and SPR. These results provide crucial insights into the structural characteristics of the KRS-LR interaction on the cell surface.

Original languageEnglish
Pages (from-to)2851-2858
Number of pages8
JournalFEBS Letters
Volume588
Issue number17
DOIs
Publication statusPublished - 2014 Aug 25

All Science Journal Classification (ASJC) codes

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

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    Cho, H. Y., Ul Mushtaq, A., Lee, J. Y., Kim, D. G., Seok, M. S., Jang, M., Han, B. W., Kim, S., & Jeon, Y. H. (2014). Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR. FEBS Letters, 588(17), 2851-2858. https://doi.org/10.1016/j.febslet.2014.06.048