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The crystal structure of arginyl-tRNA synthetase from Homo sapiens

Authors
Kim, Hyun SookCha, So YoungJo, Chang HwaHan, AhreumHwang, Kwang Yeon
Issue Date
27-6월-2014
Publisher
WILEY
Keywords
Arginyl-tRNA synthetase; L-Canavanine; L-Arginine; Rossmann fold; tRNA(Arg); Enzyme Commission number (6.1.1.19)
Citation
FEBS LETTERS, v.588, no.14, pp.2328 - 2334
Indexed
SCIE
SCOPUS
Journal Title
FEBS LETTERS
Volume
588
Number
14
Start Page
2328
End Page
2334
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/98193
DOI
10.1016/j.febslet.2014.05.027
ISSN
0014-5793
Abstract
Arginyl-tRNA synthetase (ArgRS) is a tRNA-binding protein that catalyzes the esterification of L-arginine to its cognate tRNA. L-Canavanine, a structural analog of L-arginine, has recently been studied as an anticancer agent. Here, we determined the crystal structures of the apo, L-arginine-complexed, and L-canavanine-complexed forms of the cytoplasmic free isoform of human ArgRS (hArgRS). Similar interactions were formed upon binding to L-canavanine or L-arginine, but the interaction between Tyr312 and the oxygen of the oxyguanidino group was a little bit different. Detailed conformational changes that occur upon substrate binding were explained. The hArgRS structure was also compared with previously reported homologue structures. The results presented here may provide a basis for the design of new anticancer drugs, such as L-canavanine analogs. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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