The crystal structure of arginyl-tRNA synthetase from Homo sapiens |
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Authors: | Hyun Sook Kim So Young ChaChang Hwa Jo Ahreum HanKwang Yeon Hwang |
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Institution: | Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul, Republic of Korea |
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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. |
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Keywords: | aaRS aminoacyl-tRNA synthetase hArgRS free isoform of human ArgRS PBD Protein Data Bank Nd N-terminal domain Ins1 insertion domain 1 Ins2 insertion domain 2 Cd C-terminal domain RMSD root mean square deviation |
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