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

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. Structured summary of protein interactions: KRS-ABD binds to 37LRP by surface plasmon resonance (View interaction) KRS-ABD and 37LRP bind by nuclear magnetic resonance (1, 2, 3) 37LRP and KRS-ABD bind by molecular sieving (View interaction) KRS-ABD and laminin peptide bind by nuclear magnetic resonance (View interaction) (C) 2014 Published by Elsevier B.V.