Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR |
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| Authors: | 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 |
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| Institution: | 1. College of Pharmacy, Korea University, 2511 Sejong-ro, Sejong 339-700, Republic of Korea;2. Medicinal Bioconvergence Research Center, College of Pharmacy, Seoul National University, Seoul 151-742, Republic of Korea;3. Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 151-742, Republic of Korea |
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| 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. |
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