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5a27
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Leishmania major N-myristoyltransferase in complex with a chlorophenyl inhibitor (compound 10j).== | |
| + | <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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A27 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=TUT:5-CHLORANYL-N-[2-(3-METHOXYPHENYL)ETHANIMIDOYL]-2-PIPERIDIN-4-YLOXY-BENZAMIDE'>TUT</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a28|5a28]]</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=5a27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a27 OCA], [http://pdbe.org/5a27 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a27 RCSB], [http://www.ebi.ac.uk/pdbsum/5a27 PDBsum]</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 == | ||
| + | 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> |
| + | <div class="pdbe-citations 5a27" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Glycylpeptide N-tetradecanoyltransferase]] | ||
| + | [[Category: Barker, K V]] | ||
| + | [[Category: Brannigan, J A]] | ||
| + | [[Category: Heal, W P]] | ||
| + | [[Category: Leatherbarrow, R J]] | ||
[[Category: Paape, D]] | [[Category: Paape, D]] | ||
| + | [[Category: Rackham, M D]] | ||
| + | [[Category: Smith, D F]] | ||
| + | [[Category: Tate, E W]] | ||
| + | [[Category: Wilkinson, A J]] | ||
[[Category: Yu, Z]] | [[Category: Yu, Z]] | ||
| - | [[Category: | + | [[Category: Drug design]] |
| - | [[Category: | + | [[Category: Myristoylation]] |
| - | [[Category: | + | [[Category: Transferase]] |
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Revision as of 12:58, 11 May 2016
Leishmania major N-myristoyltransferase in complex with a chlorophenyl inhibitor (compound 10j).
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