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

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

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

FEBS Lett. 2014 Aug 25;588(17):2851-8

Authors: Cho HY, Ul Mushtaq A, Lee JY, Kim DG, Seok MS, Jang M, Han BW, Kim S, Jeon YH

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.


PMID: 24983501 [PubMed - indexed for MEDLINE]



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