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

被引：12

作者：

Cho, Hye Young ^{[1
]}

Mushtaq, Ameeq Ul ^{[1
]}

Lee, Jin Young ^{[2
]}

Kim, Dae Gyu ^{[2
]}

Seok, Min Sook ^{[1
]}

Jang, Minseok ^{[3
]}

Han, Byung-Woo ^{[3
]}

Kim, Sunghoon ^{[2
]}

Jeon, Young Ho ^{[1
]}

机构：

[1] Korea Univ, Coll Pharm, Sejong 339700, South Korea

[2] Seoul Natl Univ, Coll Pharm, Med Bioconvergence Res Ctr, Seoul 151742, South Korea

[3] Seoul Natl Univ, Coll Pharm, Pharmaceut Sci Res Inst, Seoul 151742, South Korea

来源：

FEBS LETTERS | 2014年 / 588卷 / 17期

关键词：

Lysyl-tRNA synthetase; Laminin receptor; Nuclear magnetic resonance; Laminin; ACTIVATED MAST-CELLS; CRYSTAL-STRUCTURE; TRANSLATION; PRECURSOR; DOMAINS; DISEASE; COMPLEX; PROTEIN; SYSTEM; YIGSR;

D O I：

10.1016/j.febslet.2014.06.048

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：2851 / 2858

页数：8

共 32 条

[1] DOWN-REGULATION OF A 67-KDA YIGSR-BINDING PROTEIN UPON DIFFERENTIATION OF HUMAN NEUROBLASTOMA-CELLS [J].