4q2x | pdb_00004q2x

Crystal structure of Arginyl-tRNA synthetase complexed with L-canavanine

spinqualitylabelsall models 4q2x, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4q2x is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GGB Related: 4q2t, 4q2y Activity: Arginine--tRNA ligase, with EC number 6.1.1.19 Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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