4bbh: Difference between revisions
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==Plasmodium vivax N-myristoyltransferase with a bound benzothiophene inhibitor== | |||
<StructureSection load='4bbh' size='340' side='right'caption='[[4bbh]], [[Resolution|resolution]] 1.63Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4bbh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_vivax Plasmodium vivax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BBH 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]] 1.63Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NHW:2-OXOPENTADECYL-COA'>NHW</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YBN:3-METHOXYBENZYL+3-(PIPERIDIN-4-YLOXY)-1-BENZOTHIOPHENE-2-CARBOXYLATE'>YBN</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=4bbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bbh OCA], [https://pdbe.org/4bbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bbh RCSB], [https://www.ebi.ac.uk/pdbsum/4bbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bbh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A5K1A2_PLAVS A5K1A2_PLAVS] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity).[RuleBase:RU000586] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
N-Myristoyltransferase (NMT) is an attractive anti-protozoan drug target. A lead-hopping approach was utilized in the design and synthesis of novel benzo[b]thiophene-containing inhibitors of Plasmodium falciparum (Pf) and Plasmodium vivax (Pv) NMT. These inhibitors are selective against Homo sapiens NMT1 (HsNMT), have excellent ligand efficiency (LE) and display anti-parasitic activity in vitro. The binding mode of this series was determined by crystallography and shows a novel binding mode for the benzothiophene ring. | |||
Discovery of Novel and Ligand-Efficient Inhibitors of Plasmodium falciparum and Plasmodium vivax N-Myristoyltransferase.,Rackham MD, Brannigan JA, Moss DK, Yu Z, Wilkinson AJ, Holder AA, Tate EW, Leatherbarrow RJ J Med Chem. 2012 Nov 22. PMID:23170970<ref>PMID:23170970</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4bbh" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Plasmodium vivax]] | |||
[[Category: Brannigan JA]] | |||
[[Category: Holder AA]] | |||
[[Category: Leatherbarrow RJ]] | |||
[[Category: Moss DK]] | |||
[[Category: Rackham MD]] | |||
[[Category: Tate EW]] | |||
[[Category: Wilkinson AJ]] | |||
[[Category: Yu Z]] | |||
Latest revision as of 13:58, 9 May 2024
Plasmodium vivax N-myristoyltransferase with a bound benzothiophene inhibitorPlasmodium vivax N-myristoyltransferase with a bound benzothiophene inhibitor
Structural highlights
FunctionA5K1A2_PLAVS Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity).[RuleBase:RU000586] Publication Abstract from PubMedN-Myristoyltransferase (NMT) is an attractive anti-protozoan drug target. A lead-hopping approach was utilized in the design and synthesis of novel benzo[b]thiophene-containing inhibitors of Plasmodium falciparum (Pf) and Plasmodium vivax (Pv) NMT. These inhibitors are selective against Homo sapiens NMT1 (HsNMT), have excellent ligand efficiency (LE) and display anti-parasitic activity in vitro. The binding mode of this series was determined by crystallography and shows a novel binding mode for the benzothiophene ring. Discovery of Novel and Ligand-Efficient Inhibitors of Plasmodium falciparum and Plasmodium vivax N-Myristoyltransferase.,Rackham MD, Brannigan JA, Moss DK, Yu Z, Wilkinson AJ, Holder AA, Tate EW, Leatherbarrow RJ J Med Chem. 2012 Nov 22. PMID:23170970[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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