4q2y
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4q2y is ON HOLD Authors: Kim, H.S, Jo, C.H, Cha, S.Y, Han, A.R, Hwang, K.Y Description: Crystal structure of Arginyl-tRNA synthetase) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Arginyl-tRNA synthetase== | |
| + | <StructureSection load='4q2y' size='340' side='right'caption='[[4q2y]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4q2y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q2Y FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.799Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4q2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q2y OCA], [https://pdbe.org/4q2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q2y RCSB], [https://www.ebi.ac.uk/pdbsum/4q2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q2y ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SYRC_HUMAN SYRC_HUMAN] Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1.<ref>PMID:17443684</ref> | ||
| + | <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 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> | ||
| + | <div class="pdbe-citations 4q2y" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cha SY]] | ||
| + | [[Category: Han AR]] | ||
| + | [[Category: Hwang KY]] | ||
| + | [[Category: Jo CH]] | ||
| + | [[Category: Kim HS]] | ||
Current revision
Crystal structure of Arginyl-tRNA synthetase
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Categories: Homo sapiens | Large Structures | Cha SY | Han AR | Hwang KY | Jo CH | Kim HS
