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

FEBS Lett. 2014 Aug 25;588(17):2851-8. doi: 10.1016/j.febslet.2014.06.048. Epub 2014 Jun 28.

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.

Keywords: Laminin; Laminin receptor; Lysyl-tRNA synthetase; Nuclear magnetic resonance.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anticodon / metabolism
  • Cell Membrane / metabolism
  • Humans
  • Lysine-tRNA Ligase / chemistry
  • Lysine-tRNA Ligase / metabolism*
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular*
  • Peptide Fragments / metabolism
  • Protein Binding
  • Protein Structure, Tertiary
  • Receptors, Laminin / chemistry
  • Receptors, Laminin / metabolism*

Substances

  • Anticodon
  • Peptide Fragments
  • Receptors, Laminin
  • Lysine-tRNA Ligase