期刊
FEBS LETTERS
卷 588, 期 14, 页码 2328-2334出版社
WILEY
DOI: 10.1016/j.febslet.2014.05.027
关键词
Arginyl-tRNA synthetase; L-Canavanine; L-Arginine; Rossmann fold; tRNA(Arg); Enzyme Commission number (6.1.1.19)
资金
- National Research Foundation of Korea [2013-044795]
- [2012G189]
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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