View source for 5g22


==Plasmodium vivax N-myristoyltransferase in complex with a quinoline inhibitor (compound 26)==
<StructureSection load='5g22' size='340' side='right'caption='[[5g22]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5g22]] 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=5G22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G22 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]] 2.32&#8491;</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NHW:2-OXOPENTADECYL-COA'>NHW</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YN4:ETHYL+4-[(2-CYANOETHYL)SULFANYL]-6-{[6-(PIPERAZIN-1-YL)'>YN4</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=5g22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g22 OCA], [https://pdbe.org/5g22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g22 RCSB], [https://www.ebi.ac.uk/pdbsum/5g22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g22 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 ==
The parasite Plasmodium vivax is the most widely distributed cause of recurring malaria. N-Myristoyltransferase (NMT), an enzyme that catalyses the covalent attachment of myristate to the N-terminal glycine of substrate proteins, has been described as a potential target for the treatment of this disease. Herein, we report the synthesis and the structure-guided optimization of a series of quinolines with balanced activity against both Plasmodium vivax and Plasmodium falciparum N-myristoyltransferase (NMT).

Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase.,Goncalves V, Brannigan JA, Laporte A, Bell AS, Roberts SM, Wilkinson AJ, Leatherbarrow RJ, Tate EW Medchemcomm. 2017 Jan 1;8(1):191-197. doi: 10.1039/c6md00531d. Epub 2016 Nov 11. PMID:28626547<ref>PMID:28626547</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5g22" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Plasmodium vivax]]
[[Category: Bell AS]]
[[Category: Brannigan JA]]
[[Category: Goncalves V]]
[[Category: Laporte A]]
[[Category: Leatherbarrow RJ]]
[[Category: Roberts SM]]
[[Category: Tate EW]]
[[Category: Wilkinson AJ]]