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4c7h
From Proteopedia
(Difference between revisions)
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<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=4c7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c7h RCSB], [http://www.ebi.ac.uk/pdbsum/4c7h PDBsum]</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=4c7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c7h RCSB], [http://www.ebi.ac.uk/pdbsum/4c7h PDBsum]</span></td></tr> | ||
<table> | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | N-Myristoyltransferase (NMT) has been shown to be essential in Leishmania and subsequently validated as a drug target in Plasmodium. Herein, we discuss the use of antifungal NMT inhibitors as a basis for inhibitor development resulting in the first sub-micromolar peptidomimetic inhibitors of Plasmodium and Leishmania NMTs. High-resolution structures of these inhibitors with Plasmodium and Leishmania NMTs permit a comparative analysis of binding modes, and provide the first crystal structure evidence for a ternary NMT-Coenzyme A/myristoylated peptide product complex. | ||
| + | |||
| + | Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites.,Olaleye TO, Brannigan JA, Roberts SM, Leatherbarrow RJ, Wilkinson AJ, Tate EW Org Biomol Chem. 2014 Sep 18. PMID:25230674<ref>PMID:25230674</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 21:58, 1 October 2014
Leismania major N-myristoyltransferase in complex with a peptidomimetic (-NH2) molecule
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