4c68: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4c68]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_vivax Plasmodium vivax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C68 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4c68]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_vivax Plasmodium vivax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C68 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EN5:N-(10-AMINODECANOYL)-L-SERYL-N-(2-CYCLOHEXYLETHYL)-L-LYSINAMIDE'>EN5</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NHW:2-OXOPENTADECYL-COA'>NHW</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.38Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EN5:N-(10-AMINODECANOYL)-L-SERYL-N-(2-CYCLOHEXYLETHYL)-L-LYSINAMIDE'>EN5</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NHW:2-OXOPENTADECYL-COA'>NHW</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4c68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c68 OCA], [https://pdbe.org/4c68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c68 RCSB], [https://www.ebi.ac.uk/pdbsum/4c68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c68 ProSAT]</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=4c68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c68 OCA], [https://pdbe.org/4c68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c68 RCSB], [https://www.ebi.ac.uk/pdbsum/4c68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c68 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A5K1A2_PLAVS A5K1A2_PLAVS] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity).[RuleBase:RU000586] | |||
<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> | |||
<div class="pdbe-citations 4c68" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 14:09, 9 May 2024
Plasmodium vivax N-myristoyltransferase in complex with a peptidomimetic inhibitorPlasmodium vivax N-myristoyltransferase in complex with a peptidomimetic inhibitor
Structural highlights
FunctionA5K1A2_PLAVS Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity).[RuleBase:RU000586] Publication Abstract from PubMedN-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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