View source for 5g21


==Leishmania major N-myristoyltransferase in complex with a quinoline inhibitor (compound 26).==
<StructureSection load='5g21' size='340' side='right' caption='[[5g21]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5g21]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G21 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5G21 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MYA:TETRADECANOYL-COA'>MYA</scene>, <scene name='pdbligand=YN4:ETHYL+4-[(2-CYANOETHYL)SULFANYL]-6-{[6-(PIPERAZIN-1-YL)'>YN4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5g1z|5g1z]], [[5g20|5g20]], [[5g22|5g22]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycylpeptide_N-tetradecanoyltransferase Glycylpeptide N-tetradecanoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.97 2.3.1.97] </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=5g21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g21 OCA], [http://pdbe.org/5g21 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g21 RCSB], [http://www.ebi.ac.uk/pdbsum/5g21 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g21 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/Q4Q5S8_LEIMA Q4Q5S8_LEIMA]] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity). 
<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 5g21" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Glycylpeptide N-tetradecanoyltransferase]]
[[Category: Bell, A S]]
[[Category: Brannigan, J A]]
[[Category: Goncalves, V]]
[[Category: Laporte, A]]
[[Category: Leatherbarrow, R J]]
[[Category: Roberts, S M]]
[[Category: Tate, E W]]
[[Category: Wilkinson, A J]]
[[Category: Drug design]]
[[Category: Inhibitor]]
[[Category: Malaria]]
[[Category: Myristoylation]]
[[Category: Quinoline]]
[[Category: Transferase]]