Publication Abstract from PubMed
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.
The crystal structure of arginyl-tRNA synthetase from Homo sapiens.,Kim HS, Cha SY, Jo CH, Han A, Hwang KY FEBS Lett. 2014 Jun 27;588(14):2328-34. doi: 10.1016/j.febslet.2014.05.027. Epub , 2014 May 22. PMID:24859084[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
