4ye6: Difference between revisions

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 ==The crystal structure of the intact human GlnRS==
-<StructureSection load='4ye6' size='340' side='right' caption='[[4ye6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='4ye6' size='340' side='right'caption='[[4ye6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ye6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YE6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YE6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ye6]] is a 1 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=4YE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YE6 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ye8|4ye8]], [[4ye9|4ye9]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamine--tRNA_ligase Glutamine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.18 6.1.1.18] </span></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=4ye6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ye6 OCA], [https://pdbe.org/4ye6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ye6 RCSB], [https://www.ebi.ac.uk/pdbsum/4ye6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ye6 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ye6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ye6 OCA], [http://pdbe.org/4ye6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ye6 RCSB], [http://www.ebi.ac.uk/pdbsum/4ye6 PDBsum]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/SYQ_HUMAN SYQ_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry.
+[https://www.uniprot.org/uniprot/SYQ_HUMAN SYQ_HUMAN] The disease is caused by mutations affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/SYQ_HUMAN SYQ_HUMAN]] Plays a critical role in brain development.<ref>PMID:24656866</ref>
+[https://www.uniprot.org/uniprot/SYQ_HUMAN SYQ_HUMAN] Plays a critical role in brain development.<ref>PMID:24656866</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Cytosolic glutaminyl-tRNA synthetase (GlnRS) is the singular enzyme responsible for translation of glutamine codons. Compound heterozygous mutations in GlnRS cause severe brain disorders by a poorly understood mechanism. Herein, we present crystal structures of the wild type and two pathological mutants of human GlnRS, which reveal, for the first time, the domain organization of the intact enzyme and the structure of the functionally important N-terminal domain (NTD). Pathological mutations mapping in the NTD alter the domain structure, and decrease catalytic activity and stability of GlnRS, whereas missense mutations in the catalytic domain induce misfolding of the enzyme. Our results suggest that the reduced catalytic efficiency and a propensity of GlnRS mutants to misfold trigger the disease development. This report broadens the spectrum of brain pathologies elicited by protein misfolding and provides a paradigm for understanding the role of mutations in aminoacyl-tRNA synthetases in neurological diseases.
-The crystal structure of human GlnRS provides basis for the development of neurological disorders.,Ognjenovic J, Wu J, Matthies D, Baxa U, Subramaniam S, Ling J, Simonovic M Nucleic Acids Res. 2016 Feb 10. pii: gkw082. PMID:26869582<ref>PMID:26869582</ref>
+==See Also==
+*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4ye6" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Glutamine--tRNA ligase]]
+[[Category: Homo sapiens]]
-[[Category: Ling, J]]
+[[Category: Large Structures]]
-[[Category: Ognjenovic, J]]
+[[Category: Ling J]]
-[[Category: Simonovic, M]]
+[[Category: Ognjenovic J]]
-[[Category: Wu, J]]
+[[Category: Simonovic M]]
-[[Category: Aminoacyl-trna synthetase]]
+[[Category: Wu J]]
-[[Category: Class i aar]]
-[[Category: L-glutamine]]
-[[Category: Ligase]]