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4q2t
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| - | ''' | + | ==Crystal structure of Arginyl-tRNA synthetase complexed with L-arginine== |
| + | <StructureSection load='4q2t' size='340' side='right' caption='[[4q2t]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4q2t]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q2T FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4q2x|4q2x]], [[4q2y|4q2y]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginine--tRNA_ligase Arginine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.19 6.1.1.19] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q2t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q2t RCSB], [http://www.ebi.ac.uk/pdbsum/4q2t PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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 | + | 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<ref>PMID:24859084</ref> |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arginine--tRNA ligase]] | ||
| + | [[Category: Cha, S Y.]] | ||
| + | [[Category: Han, A R.]] | ||
| + | [[Category: Hwang, K Y.]] | ||
| + | [[Category: Jo, C H.]] | ||
| + | [[Category: Kim, H S.]] | ||
| + | [[Category: Arginine binding]] | ||
| + | [[Category: Arginine-trna ligase activity]] | ||
| + | [[Category: High region]] | ||
| + | [[Category: Ligase]] | ||
| + | [[Category: Trna binding]] | ||
Revision as of 07:59, 23 July 2014
Crystal structure of Arginyl-tRNA synthetase complexed with L-arginine
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