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==Leishmania major N-myristoyltransferase in complex with a quinoline inhibitor (compound 26).== | ==Leishmania major N-myristoyltransferase in complex with a quinoline inhibitor (compound 26).== | ||
<StructureSection load='5g21' size='340' side='right' caption='[[5g21]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='5g21' size='340' side='right'caption='[[5g21]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == 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:// | <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://proteopedia.org/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> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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='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:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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> | </table> | ||
== Function == | == Function == | ||
| Line 25: | Line 25: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Glycylpeptide N-tetradecanoyltransferase]] | [[Category: Glycylpeptide N-tetradecanoyltransferase]] | ||
[[Category: Large Structures]] | |||
[[Category: Bell, A S]] | [[Category: Bell, A S]] | ||
[[Category: Brannigan, J A]] | [[Category: Brannigan, J A]] | ||
Revision as of 09:35, 13 May 2020
Leishmania major N-myristoyltransferase in complex with a quinoline inhibitor (compound 26).Leishmania major N-myristoyltransferase in complex with a quinoline inhibitor (compound 26).
Structural highlights
Function[Q4Q5S8_LEIMA] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity). Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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