5a27: Difference between revisions
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==Leishmania major N-myristoyltransferase in complex with a chlorophenyl 1,2,4-oxadiazole inhibitor.== | |||
<StructureSection load='5a27' size='340' side='right'caption='[[5a27]], [[Resolution|resolution]] 1.37Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5a27]] 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=5A27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A27 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]] 1.37Å</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=TUT:5-CHLORANYL-N-[2-(3-METHOXYPHENYL)ETHANIMIDOYL]-2-PIPERIDIN-4-YLOXY-BENZAMIDE'>TUT</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=5a27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a27 OCA], [https://pdbe.org/5a27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a27 RCSB], [https://www.ebi.ac.uk/pdbsum/5a27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a27 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 == | |||
N-Myristoyltransferase (NMT) is a potential drug target in Leishmania parasites. Scaffold-hopping from published inhibitors yielded the serendipitous discovery of a chemotype selective for Leishmania donovani NMT; development led to high affinity inhibitors with excellent ligand efficiency. The binding mode was characterised by crystallography and provides a structural rationale for selectivity. | |||
Discovery of high affinity inhibitors of -myristoyltransferase.,Rackham MD, Yu Z, Brannigan JA, Heal WP, Paape D, Barker KV, Wilkinson AJ, Smith DF, Leatherbarrow RJ, Tate EW Medchemcomm. 2015 Oct 8;6(10):1761-1766. Epub 2015 Aug 19. PMID:26962429<ref>PMID:26962429</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5a27" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Leatherbarrow | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Rackham | [[Category: Large Structures]] | ||
[[Category: | [[Category: Leishmania major]] | ||
[[Category: Tate | [[Category: Barker KV]] | ||
[[Category: | [[Category: Brannigan JA]] | ||
[[Category: | [[Category: Heal WP]] | ||
[[Category: Leatherbarrow RJ]] | |||
[[Category: Paape D]] | |||
[[Category: Rackham MD]] | |||
[[Category: Smith DF]] | |||
[[Category: Tate EW]] | |||
[[Category: Wilkinson AJ]] | |||
[[Category: Yu Z]] | |||
Latest revision as of 14:35, 9 May 2024
Leishmania major N-myristoyltransferase in complex with a chlorophenyl 1,2,4-oxadiazole inhibitor.Leishmania major N-myristoyltransferase in complex with a chlorophenyl 1,2,4-oxadiazole inhibitor.
Structural highlights
FunctionQ4Q5S8_LEIMA Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity). Publication Abstract from PubMedN-Myristoyltransferase (NMT) is a potential drug target in Leishmania parasites. Scaffold-hopping from published inhibitors yielded the serendipitous discovery of a chemotype selective for Leishmania donovani NMT; development led to high affinity inhibitors with excellent ligand efficiency. The binding mode was characterised by crystallography and provides a structural rationale for selectivity. Discovery of high affinity inhibitors of -myristoyltransferase.,Rackham MD, Yu Z, Brannigan JA, Heal WP, Paape D, Barker KV, Wilkinson AJ, Smith DF, Leatherbarrow RJ, Tate EW Medchemcomm. 2015 Oct 8;6(10):1761-1766. Epub 2015 Aug 19. PMID:26962429[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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