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Characterization of the interaction between lysyl‐tRNA synthetase and laminin receptor by NMR
Author(s) -
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
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.06.048
Subject(s) - laminin , transfer rna , biochemistry , binding site , cell , biology , chemistry , stereochemistry , microbiology and biotechnology , rna , gene
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.