View source for 4ufv


==Plasmodium vivax N-myristoyltransferase in complex with a pyridyl inhibitor (compound 18)==
<StructureSection load='4ufv' size='340' side='right'caption='[[4ufv]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ufv]] 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=4UFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UFV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=31A:N-[2-(3-METHOXYPHENYL)ETHANIMIDOYL]-2-PIPERIDIN-4-YLOXY-BENZAMIDE'>31A</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOA:GLYCOLIC+ACID'>GOA</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=4ufv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ufv OCA], [https://pdbe.org/4ufv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ufv RCSB], [https://www.ebi.ac.uk/pdbsum/4ufv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ufv ProSAT]</span></td></tr>
</table>
== 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) represents an attractive drug target in parasitic infections such as malaria due to its genetic essentiality and amenability to inhibition by drug-like small molecules. Scaffold simplification from previously reported inhibitors containing bicyclic cores identified phenyl derivative 3, providing a versatile platform to study the effects of substitution on the scaffold, which yielded pyridyl 19. This molecule exhibited improved enzyme and cellular potency, and reduced lipophilicity compared to inhibitor 3. Further structure-based inhibitor design led to the discovery of 30, the most potent inhibitor in this series, which showed single-digit nM enzyme affinity and sub-muM anti-plasmodial activity.

Discovery of pyridyl-based inhibitors of -myristoyltransferase.,Yu Z, Brannigan JA, Rangachari K, Heal WP, Wilkinson AJ, Holder AA, Leatherbarrow RJ, Tate EW Medchemcomm. 2015 Oct 8;6(10):1767-1772. Epub 2015 Aug 19. PMID:26962430<ref>PMID:26962430</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ufv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Plasmodium vivax]]
[[Category: Brannigan JA]]
[[Category: Heal WP]]
[[Category: Holder AA]]
[[Category: Leatherbarrow RJ]]
[[Category: Rangachari K]]
[[Category: Tate EW]]
[[Category: Wilkinson AJ]]
[[Category: Yu Z]]