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Updated: Apr 27, 2026

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
Published on: September 28, 2020
Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR
Hye Young Cho1, Ameeq Ul Mushtaq1, Jin Young Lee2
1College of Pharmacy, Korea University, 2511 Sejong-ro, Sejong 339-700, Republic of Korea.
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.

