4Q2Y

Crystal structure of Arginyl-tRNA synthetase

4Q2Y の概要

• エントリーDOI: 10.2210/pdb4q2y/pdb
• 関連するPDBエントリー: 4Q2T 4Q2X
• 分子名称: Arginine--tRNA ligase, cytoplasmic (2 entities in total)
• 機能のキーワード: high region, arginine-trna ligase, atp binding, trna binding, arginine binding, ligase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : P54136
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 138695.45

構造登録者

Kim, H.S.,Jo, C.H.,Cha, S.Y.,Han, A.R.,Hwang, K.Y. (登録日: 2014-04-10, 公開日: 2014-07-23, 最終更新日: 2023-11-08)

主引用文献

Kim, H.S.,Cha, S.Y.,Jo, C.H.,Han, A.R.,Hwang, K.Y.
The crystal structure of arginyl-tRNA synthetase from Homo sapiens
Febs Lett., 588:2328-2334, 2014

PubMed 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.

PubMed: 24859084
DOI: 10.1016/j.febslet.2014.05.027

実験手法

X-RAY DIFFRACTION (2.799 Å)