4cyp: Difference between revisions

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-'''Unreleased structure'''
+==Leishmania major N-myristoyltransferase in complex with a pyrrolidine inhibitor.==
+<StructureSection load='4cyp' size='340' side='right' caption='[[4cyp]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4cyp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CYP FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A62:(3R)-4-(4-CHLOROPHENYL)-1-[(3S,4R)-3-(4-CHLOROPHENYL)-4-(HYDROXYMETHYL)PYRROLIDIN-1-YL]-3-HYDROXYBUTAN-1-ONE'>A62</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MYA:TETRADECANOYL-COA'>MYA</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cyn|4cyn]], [[4cyo|4cyo]], [[4cyq|4cyq]]</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=4cyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cyp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cyp RCSB], [http://www.ebi.ac.uk/pdbsum/4cyp PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Inhibitors of Leishmania NMT, a potential target for the treatment of leishmaniasis, obtained from a high-throughput screen were resynthesized to validate activity. Crystal structures bound to Leishmania major NMT were obtained and the active diastereoisomer of one of the inhibitors was identified. Based on structural insights, enzyme inhibition was increased 40-fold through hybridization of two distinct binding modes, resulting in novel, highly potent Leishmania donovani NMT inhibitors with good selectivity over the human enzyme.
-The entry 4cyp is ON HOLD  until Paper Publication
+Structure-Based Design of Potent and Selective Leishmania N-Myristoyltransferase Inhibitors.,Hutton JA, Goncalves V, Brannigan JA, Paape D, Wright MH, Waugh TM, Roberts SM, Bell AS, Wilkinson AJ, Smith DF, Leatherbarrow RJ, Tate EW J Med Chem. 2014 Sep 19. PMID:25238611<ref>PMID:25238611</ref>
-Authors: Hutton, J.A., Goncalves, V., Brannigan, J.A., Paape, D., Waugh, T., Roberts, S.M., Bell, A.S., Wilkinson, A.J., Smith, D.F., Leatherbarrow, R.J., Tate, E.W.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Leishmania major N-myristoyltransferase in complex with a pyrrolidine inhibitor.
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Glycylpeptide N-tetradecanoyltransferase]]
+[[Category: Bell, A S.]]
+[[Category: Brannigan, J A.]]
+[[Category: Goncalves, V.]]
+[[Category: Hutton, J A.]]
+[[Category: Leatherbarrow, R J.]]
+[[Category: Paape, D.]]
+[[Category: Roberts, S M.]]
+[[Category: Smith, D F.]]
+[[Category: Tate, E W.]]
+[[Category: Waugh, T.]]
+[[Category: Wilkinson, A J.]]
+[[Category: Drug design]]
+[[Category: Inhibitor]]
+[[Category: Myristoylation]]
+[[Category: Transferase]]