通过核磁共振对赖氨酰 - tRNA合成酶与层粘连蛋白受体之间相互作用的表征。
Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR.
作者信息
Cho Hye Young, Ul Mushtaq Ameeq, Lee Jin Young, Kim Dae Gyu, Seok Min Sook, Jang Minseok, Han Byung-Woo, Kim Sunghoon, Jeon Young Ho
机构信息
College of Pharmacy, Korea University, 2511 Sejong-ro, Sejong 339-700, Republic of Korea.
Medicinal Bioconvergence Research Center, College of Pharmacy, Seoul National University, Seoul 151-742, Republic of Korea.
出版信息
FEBS Lett. 2014 Aug 25;588(17):2851-8. doi: 10.1016/j.febslet.2014.06.048. Epub 2014 Jun 28.
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.
赖氨酰 - tRNA合成酶（KRS）与层粘连蛋白受体（LR/RPSA）相互作用，并在癌症转移中增强层粘连蛋白诱导的细胞迁移。在这项基于核磁共振（NMR）的研究中，我们表明KRS的反密码子结合结构域直接与37LRP的C末端区域结合，并且先前发现的抑制剂BC - K - 01和BC - K - YH16899会干扰KRS与37LRP的结合。此外，通过NMR和SPR观察到，KRS的反密码子结合结构域与层粘连蛋白结合。这些结果为细胞表面KRS - LR相互作用的结构特征提供了关键见解。
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