5dtk
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Fragments bound to the OXA-48 beta-lactamase: Compound 17== | |
| + | <StructureSection load='5dtk' size='340' side='right' caption='[[5dtk]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5dtk]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DTK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DTK FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5F3:3,5-DI(PYRIDIN-4-YL)BENZOIC+ACID'>5F3</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dva|5dva]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </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=5dtk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dtk OCA], [http://pdbe.org/5dtk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dtk RCSB], [http://www.ebi.ac.uk/pdbsum/5dtk PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The spread of antibiotic resistant bacteria is a global threat that shakes the foundations of modern healthcare. beta-Lactamases are enzymes that confer resistance to beta-lactam antibiotics in bacteria, and there is a critical need for new inhibitors of these enzymes for combination therapy together with an antibiotic. With this in mind, we have screened a library of 490 fragments to identify starting points for the development of new inhibitors of the class D beta-lactamase oxacillinase-48 (OXA-48) through surface plasmon resonance (SPR), dose-rate inhibition assays, and X-ray crystallography. Furthermore, we have uncovered structure-activity relationships and used alternate conformations from a crystallographic structure to grow a fragment into a more potent compound with a KD of 50 muM and an IC50 of 18 muM. | ||
| - | + | Screening and Design of Inhibitor Scaffolds for the Antibiotic Resistance Oxacillinase-48 (OXA-48) through Surface Plasmon Resonance Screening.,Lund BA, Christopeit T, Guttormsen Y, Bayer A, Leiros HS J Med Chem. 2016 May 20. PMID:27165692<ref>PMID:27165692</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5dtk" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Beta-lactamase]] | ||
[[Category: Christopeit, T]] | [[Category: Christopeit, T]] | ||
| - | [[Category: Lund, B | + | [[Category: Leiros, H K.S]] |
| + | [[Category: Lund, B A]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Fragment]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Inhibitor]] | ||
| + | [[Category: Lactamase]] | ||
Revision as of 22:55, 1 June 2016
Fragments bound to the OXA-48 beta-lactamase: Compound 17
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Categories: Beta-lactamase | Christopeit, T | Leiros, H K.S | Lund, B A | Complex | Fragment | Hydrolase | Inhibitor | Lactamase
