4q2x: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of Arginyl-tRNA synthetase complexed with L-canavanine==
<StructureSection load='4q2x' size='340' side='right' caption='[[4q2x]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4q2x]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q2X FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GGB:L-CANAVANINE'>GGB</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4q2t|4q2t]], [[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=4q2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q2x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q2x RCSB], [http://www.ebi.ac.uk/pdbsum/4q2x 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 entry 4q2x is ON HOLD
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>


Authors: Kim, H.S., Jo, C.H., Cha, S.Y., Han, A.R., Hwang, K.Y.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Crystal structure of Arginyl-tRNA synthetase complexed with L-canavanine
== 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: Aminoacyl-trna synthetase]]
[[Category: Arginine binding]]
[[Category: Atp binding]]
[[Category: High region]]
[[Category: Ligase]]
[[Category: Trna binding]]
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