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.
Bibliographical noteFunding Information:
This work was supported by Global Frontier Project grants [ NRF-M1AXA002-2010-0029785 and NRF-2013M3A6A4045160 ], and funded by Ministry of Science, ICP and Future Planning (MISP) of Korea.
All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology
- Cell Biology