| Literature DB >> 24983501 |
Hye Young Cho1, Ameeq Ul Mushtaq1, Jin Young Lee2, Dae Gyu Kim2, Min Sook Seok1, Minseok Jang3, Byung-Woo Han3, Sunghoon Kim2, Young Ho Jeon4.
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.Entities:
Keywords: Laminin; Laminin receptor; Lysyl-tRNA synthetase; Nuclear magnetic resonance
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Year: 2014 PMID： 24983501 DOI： 10.1016/j.febslet.2014.06.048
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124