5g21: Difference between revisions
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New page: '''Unreleased structure''' The entry 5g21 is ON HOLD Authors: Goncalves, V., Brannigan, J.A., Laporte, A., Bell, A.S., Roberts, S.M., Wilkinson, A.J., Leatherbarrow, R.J., Tate, E.W. D... |
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The | ==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=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5g21]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_major Leishmania major]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5G21 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]] 1.5Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5g21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g21 OCA], [https://pdbe.org/5g21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g21 RCSB], [https://www.ebi.ac.uk/pdbsum/5g21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g21 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5g21" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Brannigan | <references/> | ||
[[Category: Goncalves | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Leishmania major]] | ||
[[Category: | [[Category: Bell AS]] | ||
[[Category: Brannigan JA]] | |||
[[Category: Goncalves V]] | |||
[[Category: Laporte A]] | |||
[[Category: Leatherbarrow RJ]] | |||
[[Category: Roberts SM]] | |||
[[Category: Tate EW]] | |||
[[Category: Wilkinson AJ]] | |||
Latest revision as of 16:35, 26 July 2023
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
FunctionQ4Q5S8_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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