5dtk: Difference between revisions
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dva|5dva]]</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='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> | <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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dtk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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Revision as of 05:34, 13 July 2016
Fragments bound to the OXA-48 beta-lactamase: Compound 17Fragments bound to the OXA-48 beta-lactamase: Compound 17
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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