4kql
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ''' | + | ==Hin GlmU bound to WG578== |
| + | <StructureSection load='4kql' size='340' side='right' caption='[[4kql]], [[Resolution|resolution]] 2.31Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4kql]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KQL FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1SG:N-(4-{[3-(2,4-DIOXO-1,2,3,4-TETRAHYDROPYRIMIDIN-5-YL)-5-METHOXYBENZOYL]AMINO}PHENYL)PYRIDINE-2-CARBOXAMIDE'>1SG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4knr|4knr]], [[4knx|4knx]], [[4kpx|4kpx]], [[4kpz|4kpz]]</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=4kql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kql OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kql RCSB], [http://www.ebi.ac.uk/pdbsum/4kql PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | An aminoquinazoline series targeting the essential bacterial enzyme GlmU (uridyltransferase) were previously reported (Biochem. J.2012, 446, 405). In this study, we further explored SAR through a combination of traditional medicinal chemistry and structure-based drug design, resulting in a novel scaffold (benzamide) with selectivity against protein kinases. Virtual screening identified fragments that could be fused into the core scaffold, exploiting additional binding interactions and thus improving potency. These efforts resulted in a hybrid compound with target potency increased by a 1000-fold, while maintaining selectivity against selected protein kinases and an improved level of solubility and protein binding. Despite these significant improvements no significant antibacterial activity was yet observed within this class. | ||
| - | + | Rational design of inhibitors of the bacterial cell wall synthetic enzyme GlmU using virtual screening and lead-hopping.,Doig P, Boriack-Sjodin PA, Dumas J, Hu J, Itoh K, Johnson K, Kazmirski S, Kinoshita T, Kuroda S, Sato TO, Sugimoto K, Tohyama K, Aoi H, Wakamatsu K, Wang H Bioorg Med Chem. 2014 Sep 16. pii: S0968-0896(14)00604-X. doi:, 10.1016/j.bmc.2014.08.017. PMID:25262942<ref>PMID:25262942</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Boriack-Sjodin, P A.]] | ||
| + | [[Category: Doig, P.]] | ||
| + | [[Category: Kazmirski, S L.]] | ||
| + | [[Category: Beta helix]] | ||
| + | [[Category: Cell wall biosynthesis]] | ||
| + | [[Category: Small molecule fragment]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 10:43, 20 October 2014
Hin GlmU bound to WG578
| |||||||||||
